미토콘드리아

[나경실]

Mitochondrion

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organelle in eukaryotic cells responsible for respiration

Two mitochondria from mammalian lung tissue displaying their matrix and membranes as shown by electron microscopy

Cell biology

Components of a typical animal cell:

1. Nucleolus
2. Nucleus
3. Ribosome (little dots)
4. Vesicle
5. Rough endoplasmic reticulum
6. Golgi apparatus (or "Golgi body")
7. Cytoskeleton
8. Smooth endoplasmic reticulum
9. Mitochondrion
10. Vacuole
11. Cytosol (fluid that contains organelles, comprising the cytoplasm)
12. Lysosome
13. Centrosome
14. Cell membrane

Components of a typical mitochondrion

1 Outer membrane

1.1 Porin

2 Intermembrane space

2.1 Intracristal space

2.2 Peripheral space

3 Lamella

3.1 Inner membrane

3.11 Inner boundary membrane

3.12 Cristal membrane

3.2 Matrix

3.3 Cristæ

4 Mitochondrial DNA
5 Matrix granule
6 Ribosome
7 ATP synthase

The mitochondrion (/ˌmʌɪtəˈkɒndrɪən/, /-təʊ-/,^[1] plural mitochondria) is a semiautonomous double-membraneorganelle found in most eukaryoticmulticellular organisms may, however, lack mitochondria (for example, mature mammalian red blood cellsmicrosporidia, parabasalids, and diplomonads, have also reduced or transformed their mitochondria into other structures^[2] To date, only one eukaryote, Monocercomonoides, is known to have completely lost its mitochondria,^[3] and one multicellular organism, Henneguya salminicola, is known to have retained mitochondrion-related organelles in association with a complete loss of their mitochondrial genome.^[3][4][5]

The word mitochondrion comes from the Greek μίτος, mitos, "thread", and χονδρίον, chondrion, "granule"^[6] or "grain-like". Mitochondria generate most of the cell's supply of adenosine triphosphate (ATP), used as a source of chemical energy^[7] A mitochondrion is thus termed the powerhouse of the cell.^[8]

Mitochondria are commonly between 0.75 and 3 μm² in area^[9] but vary considerably in size and structure. Unless specifically stainedsignaling, cellular differentiation, and cell death, as well as maintaining control of the cell cycle and cell growth^[10] Mitochondrial biogenesis^[11][12] Mitochondria have been implicated in several human diseases, including mitochondrial disorders,^[13] cardiac dysfunction,^[14] heart failure^[15] and autism.^[16]

The number of mitochondria in a cell can vary widely by organism, tissuered blood cells have no mitochondria, whereas liver cells^[17][18] The organelle is composed of compartments that carry out specialized functions. These compartments or regions include the outer membrane, the intermembrane space, the inner membrane, and the cristae and matrix

Although most of a cell's DNA is contained in the cell nucleus, the mitochondrion has its own independent genome ("mitogenome") that shows substantial similarity to bacterial genomes^[19] Mitochondrial proteins (proteins transcribed from mitochondrial DNAcardiac mitochondria,^[20] whereas in rats^[21] The mitochondrial proteome^[22]

Contents

• 1 History of discovery and research
• 2 Origin and evolution
• 3 Structure
  • 3.1 Outer membrane
  • 3.2 Intermembrane space
  • 3.3 Inner membrane
    • 3.3.1 Cristae
  • 3.4 Matrix
  • 3.5 Mitochondria-associated ER membrane (MAM)
    • 3.5.1 Phospholipid transfer
    • 3.5.2 Calcium signaling
    • 3.5.3 Molecular basis for tethering
    • 3.5.4 Perspective
• 4 Organization and distribution
• 5 Function
  • 5.1 Energy conversion
    • 5.1.1 Pyruvate and the citric acid cycle
    • 5.1.2 NADH and FADH₂: the electron transport chain
    • 5.1.3 Heat production
  • 5.2 Storage of calcium ions
  • 5.3 Additional functions
• 6 Cellular proliferation regulation
• 7 Genome
  • 7.1 Alternative genetic code
  • 7.2 Evolution and diversity
  • 7.3 Replication and inheritance
  • 7.4 DNA repair
  • 7.5 Lack of mitochondrial DNA
• 8 Population genetic studies
• 9 Dysfunction and disease
  • 9.1 Mitochondrial diseases
  • 9.2 Possible relationships to aging
• 10 In popular culture
• 11 See also
• 12 References
• 13 External links

History of discovery and research[edit]

The first observations of intracellular structures that probably represented mitochondria were published in the 1840s.^[23] Richard Altmann^[23][24] The term "mitochondria" was coined by Carl Benda in 1898.^[23][25] Leonor Michaelis discovered that Janus green can be used as a supravital stainFriedrich Meves, made the first recorded observation of mitochondria in plants in cells of the white waterlily, Nymphaea alba^[23][26] and in 1908, along with Claudius Regaud^[23] In 1913, particles from extracts of guinea-pig liver were linked to respiration by Otto Heinrich WarburgHeinrich Otto WielandDavid Keilin discovered cytochromes, that the respiratory chain^[23]

In 1939, experiments using minced muscle cells demonstrated that cellular respiration using one oxygen atom can form two adenosine triphosphate (ATP) molecules, and, in 1941, the concept of the phosphate bonds of ATP being a form of energy in cellular metabolism was developed by Fritz Albert Lipmann^[23] The introduction of tissue fractionation by Albert Claudecytochrome oxidaseEugene Kennedy and Albert Lehninger discovered in 1948 that mitochondria are the site of oxidative phosphorylation^[23]

The first high-resolution electron micrographs^[23] This led to a more detailed analysis of the structure of the mitochondria, including confirmation that they were surrounded by a membrane. It also showed a second membrane inside the mitochondria that folded up in ridges dividing up the inner chamber and that the size and shape of the mitochondria varied from cell to cell.

The popular term "powerhouse of the cell" was coined by Philip Siekevitz^[8]

In 1967, it was discovered that mitochondria contained ribosomes^[27] In 1968, methods were developed for mapping the mitochondrial genes, with the genetic and physical map of yeast mitochondrial DNA being completed in 1976.^[23]

Origin and evolution[edit]

Main article: Endosymbiotic theory

There are two hypotheses about the origin of mitochondria: endosymbiotic and autogenousprokaryotic cells, capable of implementing oxidative mechanisms that were not possible for eukaryotic cells; they became endosymbionts^[28] In the autogenous hypothesis, mitochondria were born by splitting off a portion of DNA from the nucleus of the eukaryotic cell at the time of divergence with the prokaryotes; this DNA portion would have been enclosed by membranes, which could not be crossed by proteins. Since mitochondria have many features in common with bacteria^[28][29]

A mitochondrion contains DNA, which is organized as several copies of a single, usually circular chromosomeredoxCoRR hypothesisgenome codes for some RNAs of ribosomes, and the 22 tRNAs necessary for the translation of mRNAsRickettsia.^[30][31] However, the exact relationship of the ancestor of mitochondria to the alphaproteobacteria^[32] For example, it has been suggested that the SAR11 clade of bacteria shares a relatively recent common ancestor with the mitochondria,^[33] while phylogenomic analyses indicate that mitochondria evolved from a proteobacteria lineage is closely related to or a member of alphaproteobacteria^[34][35]

Schematic ribosomal RNA phylogeny of Alphaproteobacteria

  Magnetococcidae  

  Magnetococcus marinus

  Caulobacteridae  

	Rhodospirillales, Sphingomonadales,   Rhodobacteraceae, Rhizobiales, etc.
	Holosporales

  Rickettsidae  

  Pelagibacterales  

  Pelagibacteraceae  

	Pelagibacter

  Subgroups Ib, II, IIIa, IIIb, IV and V

  Proto-mitochondria

  Anaplasmataceae  

	Ehrlichia
	Anaplasma

  Wolbachia

  Neorickettsia

  Midichloriaceae  

	Midichloria

  Rickettsiaceae  

	Rickettsia
	Orientia

The cladogram of Rickettsidae has been inferred by Ferla et al. ^[36] from the comparison of 16S + 23S

The ribosomes coded for by the mitochondrial DNA are similar to those from bacteria in size and structure.^[37] They closely resemble the bacterial 70S ribosome and not the 80S cytoplasmic ribosomes, which are coded for by nuclear

The endosymbiotic relationship of mitochondria with their host cells was popularized by Lynn Margulis^[38] The endosymbiotic hypothesis suggests that mitochondria descended from bacteria that somehow survived endocytosis by another cell, and became incorporated into the cytoplasmrespiration in host cells that had relied on glycolysis and fermentation^[39][40] A few groups of unicellular eukaryotes have only vestigial mitochondria or derived structures: the microsporidians, metamonads, and archamoebae^[41] These groups appear as the most primitive eukaryotes on phylogenetic trees constructed using rRNAlong-branch attractionmitosomes and hydrogenosomes^[2] By this, mitochondria, hydrogenosomes, mitosomes, and related organelles as found in some loriciferaSpinoloricus)^[42][43] and myxozoaHenneguya zschokkei) are together classified as MROs, mitochondrion-related organelles.^[44]

Monocercomonoides appear to have lost their mitochondria completely and at least some of the mitochondrial functions seem to be carried out by cytoplasmic proteins now.^[45]

Structure[edit]

1 Outer membrane

1.1 Porins

2 Intermembrane space

2.1 Intracristal space

2.2 Peripheral space

3 Lamellæ

3.1 Inner membrane

3.11 Inner boundary membrane

3.12 Cristal membrane

3.2 Matrix

3.3 Cristæ

4 Mitochondrial DNA

5 Matix granule

6 Ribosome

7 ATP synthase

Edit · Source image

Mitochondrion ultrastructure (interactive diagram) A mitochondrion has a double membrane; the inner one contains its chemiosmotic^[46] and their intermembrane space is quite thin.

A mitochondrion contains outer and inner membranes composed of phospholipid bilayers and proteins^[17] The two membranes have different properties. Because of this double-membraned organization, there are five distinct parts to a mitochondrion. They are:

1. the outer mitochondrial membrane,
2. the intermembrane space (the space between the outer and inner membranes),
3. the inner mitochondrial membrane,
4. the cristae space (formed by infoldings of the inner membrane), and
5. the matrix

Mitochondria stripped of their outer membrane are called mitoplasts

Outer membrane[edit]

The outer mitochondrial membrane, which encloses the entire organelle, is 60 to 75 angstromscell membraneintegral membrane proteins called porinsvoltage-dependent anion channelVDAC is the primary transporter of nucleotides, ions and metabolites between the cytosol^[47][48] It is formed as a beta barrel that spans the outer membrane, similar to that in the gram-negative bacterial^[49] Larger proteins can enter the mitochondrion if a signaling sequence at their N-terminus binds to a large multisubunit protein called translocase in the outer membrane, which then actively moves^[50] Mitochondrial pro-proteins

The outer membrane also contains enzymes involved in such diverse activities as the elongation of fatty acids, oxidation of epinephrine, and the degradation of tryptophanmonoamine oxidase, rotenonekynurenine hydroxylaseligase^[51] The mitochondrial outer membrane can associate with the endoplasmic reticulum (ER) membrane, in a structure called MAM (mitochondria-associated ER-membrane). This is important in the ER-mitochondria calcium signaling and is involved in the transfer of lipids between the ER and mitochondria.^[52] Outside the outer membrane there are small (diameter: 60Å) particles named sub-units of Parson.

Intermembrane space[edit]

The mitochondrial intermembrane space is the space between the outer membrane and the inner membrane. It is also known as perimitochondrial space. Because the outer membrane is freely permeable to small molecules, the concentrations of small molecules, such as ions and sugars, in the intermembrane space is the same as in the cytosol^[17] However, large proteins must have a specific signaling sequence to be transported across the outer membrane, so the protein composition of this space is different from the protein composition of the cytosolcytochrome c^[51]

Inner membrane[edit]

Main article: Inner mitochondrial membrane

The inner mitochondrial membrane contains proteins with five types of functions:^[17]

1. Those that perform the redox reactions of oxidative phosphorylation
2. ATP synthase, which generates ATP in the matrix
3. Specific transport proteins that regulate metabolite passage into and out of the mitochondrial matrix
4. Protein import machinery
5. Mitochondrial fusion and fission protein

It contains more than 151 different polypeptides^[17] In addition, the inner membrane is rich in an unusual phospholipid, cardiolipincow^[53] Cardiolipin contains four fatty acids rather than two, and may help to make the inner membrane impermeable.^[17] Unlike the outer membrane, the inner membrane does not contain porins, and is highly impermeable to all molecules. Almost all ions and molecules require special membrane transporters to enter or exit the matrix. Proteins are ferried into the matrix via the translocase of the inner membrane (TIM) complex or via Oxa1^[50] In addition, there is a membrane potential across the inner membrane, formed by the action of the enzymes of the electron transport chain

Cristae[edit]

Cross-sectional image of cristae in rat liver mitochondrion to demonstrate the likely 3D structure and relationship to the inner membrane

Main article: Cristae

The inner mitochondrial membrane is compartmentalized into numerous cristae^[54]. These folds are studded with small round bodies known as F₁ particleschemiosmotic^[55]

One recent mathematical modeling study has suggested that the optical properties of the cristae in filamentous mitochondria may affect the generation and propagation of light within the tissue.^[56]

Matrix[edit]

Main article: Mitochondrial matrix

The matrix is the space enclosed by the inner membrane. It contains about 2/3 of the total proteins in a mitochondrion.^[17] The matrix is important in the production of ATP with the aid of the ATP synthase contained in the inner membrane. The matrix contains a highly concentrated mixture of hundreds of enzymes, special mitochondrial ribosomes, tRNA, and several copies of the mitochondrial DNA genomepyruvate and fatty acids, and the citric acid cycle^[17] The DNA molecules are packaged into nucleoids by proteins, one of which is TFAM^[57]

Mitochondria have their own genetic material, and the machinery to manufacture their own RNAs and proteins (see: protein biosynthesis). A published human mitochondrial DNA sequence revealed 16,569 base pairs encoding 37 genes: 22 tRNA, 2 rRNA, and 13 peptide^[58] The 13 mitochondrial peptides in humans are integrated into the inner mitochondrial membrane, along with proteins encoded by genes that reside in the host cell's nucleus

Mitochondria-associated ER membrane (MAM)[edit]

Main article: Mitochondria associated membranes (MAM)

The mitochondria-associated ER membrane (MAM) is another structural element that is increasingly recognized for its critical role in cellular physiology and homeostasis^[59] Physical coupling between these two organelles had previously been observed in electron micrographs and has more recently been probed with fluorescence microscopy^[59] Such studies estimate that at the MAM, which may comprise up to 20% of the mitochondrial outer membrane, the ER and mitochondria are separated by a mere 10–25 nm and held together by protein tethering complexes.^[59][52][60]

Purified MAM from subcellular fractionation has been shown to be enriched in enzymes involved in phospholipid exchange, in addition to channels associated with Ca²⁺ signaling.^[59][60] These hints of a prominent role for the MAM in the regulation of cellular lipid stores and signal transduction have been borne out, with significant implications for mitochondrial-associated cellular phenomena, as discussed below. Not only has the MAM provided insight into the mechanistic basis underlying such physiological processes as intrinsic apoptosis and the propagation of calcium signaling, but it also favors a more refined view of the mitochondria. Though often seen as static, isolated 'powerhouses' hijacked for cellular metabolism through an ancient endosymbiotic event, the evolution of the MAM underscores the extent to which mitochondria have been integrated into overall cellular physiology, with intimate physical and functional coupling to the endomembrane system.

Phospholipid transfer[edit]

The MAM is enriched in enzymes involved in lipid biosynthesis, such as phosphatidylserine synthase on the ER face and phosphatidylserine decarboxylase on the mitochondrial face.^[61][62] Because mitochondria are dynamic organelles constantly undergoing fission and fusion^[63][64] But mitochondria are not only a destination for the phospholipids they finish synthesis of; rather, this organelle also plays a role in inter-organelle trafficking of the intermediates and products of phospholipid biosynthetic pathways, ceramide and cholesterol metabolism, and glycosphingolipid anabolism.^[62][64]

Such trafficking capacity depends on the MAM, which has been shown to facilitate transfer of lipid intermediates between organelles.^[61] In contrast to the standard vesicular mechanism of lipid transfer, evidence indicates that the physical proximity of the ER and mitochondrial membranes at the MAM allows for lipid flipping between opposed bilayers.^[64] Despite this unusual and seemingly energetically unfavorable mechanism, such transport does not require ATP.^[64] Instead, in yeast, it has been shown to be dependent on a multiprotein tethering structure termed the ER-mitochondria encounter structure, or ERMES, although it remains unclear whether this structure directly mediates lipid transfer or is required to keep the membranes in sufficiently close proximity to lower the energy barrier for lipid flipping.^[64][65]

The MAM may also be part of the secretory pathway, in addition to its role in intracellular lipid trafficking. In particular, the MAM appears to be an intermediate destination between the rough ER and the Golgi in the pathway that leads to very-low-density lipoprotein^[62][66] The MAM thus serves as a critical metabolic and trafficking hub in lipid metabolism.

Calcium signaling[edit]

A critical role for the ER in calcium signaling was acknowledged before such a role for the mitochondria was widely accepted, in part because the low affinity of Ca²⁺ channels localized to the outer mitochondrial membrane seemed to contradict this organelle's purported responsiveness to changes in intracellular Ca²⁺ flux.^[59][67] But the presence of the MAM resolves this apparent contradiction: the close physical association between the two organelles results in Ca²⁺ microdomains at contact points that facilitate efficient Ca²⁺ transmission from the ER to the mitochondria.^[59] Transmission occurs in response to so-called "Ca²⁺ puffs" generated by spontaneous clustering and activation of IP3R, a canonical ER membrane Ca²⁺ channel.^[59][52]

The fate of these puffs—in particular, whether they remain restricted to isolated locales or integrated into Ca²⁺ waves for propagation throughout the cell—is determined in large part by MAM dynamics. Although reuptake of Ca²⁺ by the ER (concomitant with its release) modulates the intensity of the puffs, thus insulating mitochondria to a certain degree from high Ca²⁺ exposure, the MAM often serves as a firewall that essentially buffers Ca²⁺ puffs by acting as a sink into which free ions released into the cytosol can be funneled.^[59][68][69] This Ca²⁺ tunneling occurs through the low-affinity Ca²⁺ receptor VDAC1, which recently has been shown to be physically tethered^[59][52][70] The ability of mitochondria to serve as a Ca²⁺ sink is a result of the electrochemical gradient generated during oxidative phosphorylation, which makes tunneling of the cation an exergonic process.^[70] Normal, mild calcium influx from cytosol into the mitochondrial matrix causes transient depolarization that is corrected by pumping out protons.

But transmission of Ca²⁺ is not unidirectional; rather, it is a two-way street.^[67] The properties of the Ca²⁺ pump SERCA and the channel IP3R present on the ER membrane facilitate feedback regulation coordinated by MAM function. In particular, the clearance of Ca²⁺ by the MAM allows for spatio-temporal patterning of Ca²⁺ signaling because Ca²⁺ alters IP3R activity in a biphasic manner.^[59] SERCA is likewise affected by mitochondrial feedback: uptake of Ca²⁺ by the MAM stimulates ATP production, thus providing energy that enables SERCA to reload the ER with Ca²⁺ for continued Ca²⁺ efflux at the MAM.^[68][70] Thus, the MAM is not a passive buffer for Ca²⁺ puffs; rather it helps modulate further Ca²⁺ signaling through feedback loops that affect ER dynamics.

Regulating ER release of Ca²⁺ at the MAM is especially critical because only a certain window of Ca²⁺ uptake sustains the mitochondria, and consequently the cell, at homeostasis. Sufficient intraorganelle Ca²⁺ signaling is required to stimulate metabolism by activating dehydrogenase enzymes critical to flux through the citric acid cycle.^[71] However, once Ca²⁺ signaling in the mitochondria passes a certain threshold, it stimulates the intrinsic pathway of apoptosis in part by collapsing the mitochondrial membrane potential required for metabolism.^[59] Studies examining the role of pro- and anti-apoptotic factors support this model; for example, the anti-apoptotic factor Bcl-2 has been shown to interact with IP3Rs to reduce Ca²⁺ filling of the ER, leading to reduced efflux at the MAM and preventing collapse of the mitochondrial membrane potential post-apoptotic stimuli.^[59] Given the need for such fine regulation of Ca²⁺ signaling, it is perhaps unsurprising that dysregulated mitochondrial Ca²⁺ has been implicated in several neurodegenerative diseases, while the catalogue of tumor suppressors includes a few that are enriched at the MAM.^[70]

Molecular basis for tethering[edit]

Recent advances in the identification of the tethers^[64] However, a homologue of the ERMES complex has not yet been identified in mammalian cells. Other proteins implicated in scaffolding likewise have functions independent of structural tethering at the MAM; for example, ER-resident and mitochondrial-resident mitofusins form heterocomplexes that regulate the number of inter-organelle contact sites, although mitofusins were first identified for their role in fission and fusion^[59] Glucose-related protein 75 (grp75) is another dual-function protein. In addition to the matrix pool of grp75, a portion serves as a chaperone that physically links the mitochondrial and ER Ca²⁺ channels VDAC and IP3R for efficient Ca²⁺ transmission at the MAM.^[59][52] Another potential tether is Sigma-1R^[72][73]

Model of the yeast multimeric tethering complex, ERMES

Perspective[edit]

The MAM is a critical signaling, metabolic, and trafficking hub in the cell that allows for the integration of ER and mitochondrial physiology. Coupling between these organelles is not simply structural but functional as well and critical for overall cellular physiology and homeostasis. The MAM thus offers a perspective on mitochondria that diverges from the traditional view of this organelle as a static, isolated unit appropriated for its metabolic capacity by the cell^[74]. Instead, this mitochondrial-ER interface emphasizes the integration of the mitochondria, the product of an endosymbiotic event, into diverse cellular processes. Recently it has also been shown, that mitochondria and MAM-s in neurons are anchored to specialised intercellular communication sites (so called somatic-junctions). Microglial processes monitor and protect neuronal functions at these sites, and MAM-s are supposed to have an important role in this type of cellular quality-control^[75].

Organization and distribution[edit]

Typical mitochondrial network (green) in two human cells (HeLa cells)

Mitochondria (and related structures) are found in all eukaryotes (except two—the Oxymonad Monocercomonoides and Henneguya salminicola).^{[3][3][76][5][77]} Although commonly depicted as bean-like structures they form a highly dynamic network in the majority of cells where they constantly undergo fission and fusion^[78] Mitochondria vary in number and location according to cell type. A single mitochondrion is often found in unicellular organisms. Conversely, the chondriome size of human liver cells is large, with about 1000–2000 mitochondria per cell, making up 1/5 of the cell volume.^[17] The mitochondrial content of otherwise similar cells can vary substantially in size and membrane potential,^[79] with differences arising from sources including uneven partitioning at cell divisions, leading to extrinsic differences^[80] The mitochondria can be found nestled between myofibrils of muscle or wrapped around the sperm flagellum^[17] Often, they form a complex 3D branching network inside the cell with the cytoskeleton^[81] different structures of the mitochondrial network may afford the population a variety of physical, chemical, and signalling advantages or disadvantages.^[82] Mitochondria in cells are always distributed along microtubules and the distribution of these organelles is also correlated with the endoplasmic reticulum.^[83] Recent evidence suggests that vimentin^[84]

Function[edit]

The most prominent roles of mitochondria are to produce the energy currency of the cell, ATPADP), through respiration, and to regulate cellular metabolism^[18] The central set of reactions involved in ATP production are collectively known as the citric acid cycle, or the Krebs

Energy conversion[edit]

A dominant role for the mitochondria is the production of ATPglucose: pyruvate, and NADH^[18] This type of cellular respiration known as aerobic respiration, is dependent on the presence of oxygen^[85] When oxygen is limited, the glycolytic products will be metabolized by anaerobic fermentation^[18] The production of ATP from glucose and oxygen has an approximately 13-times higher yield during aerobic respiration compared to fermentation.^[86] Plant mitochondria can also produce a limited amount of ATP without oxygen by using the alternate substrate nitrite^[87] ATP crosses out through the inner membrane with the help of a specific protein

Pyruvate and the citric acid cycle[edit]

Main articles: Pyruvate dehydrogenase, Pyruvate carboxylase, and Citric acid cycle

Pyruvate molecules produced by glycolysis are actively transported across the inner mitochondrial membrane, and into the matrix where they can either be oxidized and combined with coenzyme A to form CO₂, acetyl-CoA, and NADH,^[18] or they can be carboxylated (by pyruvate carboxylaseanaplerotic reactionmuscle^[88]

In the citric acid cycle, all the intermediates (e.g. citrate, iso-citrate, alpha-ketoglutarate, succinate, fumarate, malate and oxaloacetate) are regenerated during each turn of the cycle. Adding more of any of these intermediates to the mitochondrion therefore means that the additional amount is retained within the cycle, increasing all the other intermediates as one is converted into the other. Hence, the addition of any one of them to the cycle has an anaplerotic effect, and its removal has a cataplerotic effect. These anaplerotic and cataplerotic reactions will, during the course of the cycle, increase or decrease the amount of oxaloacetate available to combine with acetyl-CoA to form citric acid. This in turn increases or decreases the rate of ATP^[88]

Acetyl-CoA, on the other hand, derived from pyruvate oxidation, or from the beta-oxidation of fatty acids₂ and water, with the energy thus released captured in the form of ATP.^[88]

In the liver, the carboxylation of cytosolicgluconeogenic pathway, which converts lactatealanine into glucose,^[18][88] under the influence of high levels of glucagon and/or epinephrine^[88] Here, the addition of oxaloacetate to the mitochondrion does not have a net anaplerotic effect, as another citric acid cycle intermediate (malate) is immediately removed from the mitochondrion to be converted into cytosolic oxaloacetate, which is ultimately converted into glucose, in a process that is almost the reverse of glycolysis^[88]

The enzymes of the citric acid cycle are located in the mitochondrial matrix, with the exception of succinate dehydrogenase^[89] The citric acid cycle oxidizes the acetyl-CoA to carbon dioxide, and, in the process, produces reduced cofactors (three molecules of NADH and one molecule of FADH₂) that are a source of electrons for the electron transport chain, and a molecule of GTP^[18]

NADH and FADH₂: the electron transport chain[edit]

Main articles: Electron transport chain and Oxidative phosphorylation

Electron transport chain in the mitochondrial intermembrane space

The electrons from NADH and FADH₂ are transferred to oxygen (O₂), an energy-rich molecule,^[85] and hydrogen (protons) in several steps via the electron transport chain. NADH and FADH₂ molecules are produced within the matrix via the citric acid cycle but are also produced in the cytoplasm by glycolysisReducing equivalents from the cytoplasm can be imported via the malate-aspartate shuttle system of antiporter proteins or feed into the electron transport chain using a glycerol phosphate shuttle^[18] Protein complexes in the inner membrane (NADH dehydrogenase (ubiquinone), cytochrome c reductase, and cytochrome c oxidase) perform the transfer and the incremental release of energy is used to pump protons (H⁺) into the intermembrane space. This process is efficient, but a small percentage of electrons may prematurely reduce oxygen, forming reactive oxygen species such as superoxide^[18] This can cause oxidative stress^[90]

As the proton concentration increases in the intermembrane space, a strong electrochemical gradientATP synthase complex, and their potential energy is used to synthesize ATP from ADP and inorganic phosphate (P_i).^[18] This process is called chemiosmosis, and was first described by Peter Mitchell,^[91][92] who was awarded the 1978 Nobel Prize in ChemistryPaul D. Boyer and John E. Walker^[93]

Heat production[edit]

Under certain conditions, protons can re-enter the mitochondrial matrix without contributing to ATP synthesis. This process is known as proton leak or mitochondrial uncoupling and is due to the facilitated diffusion^[18] The process is mediated by a proton channel called thermogenin, or UCP1^[94] Thermogenin is a 33 kDa^[95] Thermogenin is primarily found in brown adipose tissue^[94]

Storage of calcium ions[edit]

Transmission electron micrograph of a chondrocyte

The concentrations of free calcium in the cell can regulate an array of reactions and is important for signal transductionstore calcium^{[96] [97]} In fact, their ability to rapidly take in calcium for later release makes them very good "cytosolic buffers" for calcium.^{[98][99][100]} The endoplasmic reticulum (ER) is the most significant storage site of calcium,^[67] and there is a significant interplay between the mitochondrion and ER with regard to calcium.^[101] The calcium is taken up into the matrix by the mitochondrial calcium uniporter on the inner mitochondrial membrane^[102] It is primarily driven by the mitochondrial membrane potential^[97] Release of this calcium back into the cell's interior can occur via a sodium-calcium exchange protein or via "calcium-induced-calcium-release" pathways.^[102] This can initiate calcium spikes or calcium waves with large changes in the membrane potentialsecond messenger system proteins that can coordinate processes such as neurotransmitter release in nerve cells and release of hormones^[103]

Ca²⁺ influx to the mitochondrial matrix has recently been implicated as a mechanism to regulate respiratory bioenergeticsoxidative stress^[104] In neurons, concomitant increases in cytosolic and mitochondrial calcium act to synchronize neuronal activity with mitochondrial energy metabolism. Mitochondrial matrix calcium levels can reach the tens of micromolar levels, which is necessary for the activation of isocitrate dehydrogenase, one of the key regulatory enzymes of the Krebs cycle^[105]

Additional functions[edit]

Mitochondria play a central role in many other metabolic tasks, such as:

• Signaling through mitochondrial reactive oxygen species^[106]
• Regulation of the membrane potential^[18]
• Apoptosis^[107]
• Calcium signaling (including calcium-evoked apoptosis)^[108]
• Regulation of cellular metabolism^[10]
• Certain heme synthesis reactions^[109] (see also: porphyrin)
• Steroid^[98]
• Hormonal signaling ^[110] Mitochondria are sensitive and responsive to hormones, in part by the action of mitochondrial estrogen receptors (mtERs). These receptors have been found in various tissues and cell types, including brain ^[111] and heart ^[112]
• Immune signaling ^[113]
• Neuronal mitochondria also contribute to cellular quality control by reporting neuronal status towards microglia through specialised somatic-junctions ^[114]

Some mitochondrial functions are performed only in specific types of cells. For example, mitochondria in liver cells contain enzymes that allow them to detoxify ammoniamitochondrial diseases

Cellular proliferation regulation[edit]

The relationship between cellular proliferation and mitochondria has been investigated using cervical cancer HeLaAdenosine triphosphate) in order to synthesize bioactive compounds such as lipids, proteins, and nucleotides^[115] The majority of ATP in tumor cells is generated via the oxidative phosphorylation^[116] Interference with OxPhos have shown to cause cell cycle arrest suggesting that mitochondria play a role in cell proliferation.^[116] Mitochondrial ATP production is also vital for cell division and differentiation in infection ^[117] in addition to basic functions in the cell including the regulation of cell volume, solute concentration^{[118][119][120]} ATP levels differ at various stages of the cell cycle suggesting that there is a relationship between the abundance of ATP and the cell's ability to enter a new cell cycle.^[121] ATP's role in the basic functions of the cell make the cell cycle^[121] The variation in ATP levels at different stages of the cell cycle support the hypothesis that mitochondria play an important role in cell cycle regulation.^[121] Although the specific mechanisms between mitochondria and the cell cycle regulation is not well understood, studies have shown that low energy cell cycle checkpoints monitor the energy capability before committing to another round of cell division.^[10]

Genome[edit]

The circular 16,569 bp human mitochondrial genome encoding 37 genes, i.e., 28 on the H-strand and 9 on the L-strand.

Main article: Mitochondrial DNA

Mitochondria contain their own genome, an indication that they are derived from bacteria through endosymbiosis

The human mitochondrial genome is a circular DNA molecule of about 16 kilobases^[122] It encodes 37 genes: 13 for subunits of respiratory complexes I, III, IV and V, 22 for mitochondrial tRNA (for the 20 standard amino acids, plus an extra gene for leucine and serine), and 2 for rRNA^[122] One mitochondrion can contain two to ten copies of its DNA.^[123]

As in prokaryotes, there is a very high proportion of coding DNA and an absence of repeats. Mitochondrial genes are transcribed as multigenic transcripts, which are cleaved and polyadenylated to yield mature mRNAscell nucleus^[58] The exact number of genes encoded by the nucleus and the mitochondrial genome^[124] In general, mitochondrial DNA lacks introns, as is the case in the human mitochondrial genome;^[58] however, introns have been observed in some eukaryotic mitochondrial DNA,^[125] such as that of yeast^[126] and protists,^[127] including Dictyostelium discoideum.^[128] Between protein-coding regions, tRNAs are present. During transcription, the tRNAs acquire their characteristic L-shape that gets recognized and cleaved by specific enzymes. Mitochondrial tRNA genes have different sequences from the nuclear tRNAs but lookalikes of mitochondrial tRNAs have been found in the nuclear chromosomes with high sequence similarity.^[129]

In animals, the mitochondrial genome is typically a single circular chromosome that is approximately 16 kb long and has 37 genes. The genes, while highly conserved, may vary in location. Curiously, this pattern is not found in the human body louse (Pediculus humanus). Instead, this mitochondrial genome is arranged in 18 minicircular chromosomes, each of which is 3–4 kb long and has one to three genes.^[130] This pattern is also found in other sucking lice, but not in chewing lice

Alternative genetic code[edit]

While slight variations on the standard genetic code had been predicted earlier,^[131] none was discovered until 1979, when researchers studying human mitochondrial genes^[132] However, the mitochondria of many other eukaryotes, including most plants, use the standard code.^[133] Many slight variants have been discovered since,^[134] including various alternative mitochondrial codes.^[135] Further, the AUA, AUC, and AUU codons are all allowable start codons.

Exceptions to the standard genetic code in mitochondria^[17]

Organism	Codon	Standard	Mitochondria
Mammals	AGA, AGG	Arginine	Stop codon
Invertebrates	AGA, AGG	Arginine	Serine
Fungi	CUA	Leucine	Threonine
All of the above	AUA	Isoleucine	Methionine
	UGA	Stop codon	Tryptophan

Some of these differences should be regarded as pseudo-changes in the genetic code due to the phenomenon of RNA editingtryptophan and not arginine; however, the codon in the processed RNA was discovered to be the UGG codon, consistent with the standard genetic code^[136] Of note, the arthropod mitochondrial genetic code has undergone parallel evolution within a phylum, with some organisms uniquely translating AGG to lysine.^[137]

Evolution and diversity[edit]

Mitochondrial genomes have far fewer genes than the bacterianucleus^[122] This is thought to be relatively common over evolutionary time. A few organisms, such as the Cryptosporidium, actually have mitochondria that lack any DNA, presumably because all their genes have been lost or transferred.^[138] In Cryptosporidium, the mitochondria have an altered ATP generation system that renders the parasite resistant to many classical mitochondrial inhibitors such as cyanide, azide, and atovaquone^[138]

Replication and inheritance[edit]

Mitochondria divide by binary fission^[139] The regulation of this division differs between eukaryotes. In many single-celled eukaryotes, their growth and division are linked to the cell cyclecytoplasmmitochondrial fusion and fission^[140]

The hypothesis of mitochondrial binary fission has relied on the visualization by fluorescence microscopy and conventional transmission electron microscopy^[which?] in verifying mitochondrial division. Cryo-electron tomography^[141]

An individual's mitochondrial genes are not inherited by the same mechanism as nuclear genesegg cell is fertilized by a sperm, the egg nucleus and sperm nucleus each contribute equally to the genetic makeup of the zygote^[142] Instead, paternal mitochondria are marked with ubiquitin to select them for later destruction inside the embryo^[143] The egg cell contains relatively few mitochondria, but it is these mitochondria that survive and divide to populate the cells of the adult organism. Mitochondria are, therefore, in most cases inherited only from mothers, a pattern known as maternal inheritanceconiferous plants, although not in pine trees and yews^[144] For Mytilids^{[145][146][147]} It has been suggested that it occurs at a very low level in humans.^[148] It was suggested in 2012, in an article in Current Biology, that mitochondria that shorten male lifespan stay in the system because they are inherited only through the mother. By contrast, natural selection^[149] Dr Tom Kirkwood, professor of ageing at Newcastle University, commented on the article "I certainly don't think this is a discovery that explains why women live five-to-six years longer than men."

Uniparental inheritance leads to little opportunity for genetic recombination^[123] For this reason, mitochondrial DNA is usually thought to reproduce by binary fission^[150] Further, evidence suggests that animal mitochondria can undergo recombination.^[151] The data are a bit more controversial in humans, although indirect evidence of recombination exists.^[152][153] If recombination does not occur, the whole mitochondrial DNA sequence represents a single haplotype

Entities undergoing uniparental inheritance and with little to no recombination may be expected to be subject to Muller's ratchetmtDNA bottleneckstochastic processes in the cellmutant load^{[154][155][156]} with a recent mathematical and experimental metastudy providing evidence for a combination of random partitioning of mtDNAs at cell divisions and random turnover of mtDNA molecules within the cell.^[157]

DNA repair[edit]

Mitochondria can repair oxidative DNA damage by mechanisms that are analogous to those occurring in the cell nucleusmtDNA repair are encoded by nuclear genesDNA repair pathways in mammalian mitochondria include base excision repairmismatch repair^[158][159] Also DNA damages may be bypassed, rather than repaired, by translesion synthesis.

Of the several DNA repair process in mitochondria, the base excision repair^[159] Base excision repair is carried out by a sequence of enzymatic catalyzed steps that include recognition and excision of a damaged DNA base, removal of the resulting abasic site, end processing, gap filling and ligation. A common damage in mtDNA that is repaired by base excision repair is 8-oxoguanine produced by the oxidation of guanine^[160]

Double-strand breaks can be repaired by homologous recombinational repair in both mammalian mtDNA^[161] and plant mtDNA.^[162] Double-strand breaks in mtDNA can also be repaired by microhomology-mediated end joining^[163] Although there is evidence for the repair processes of direct reversal and mismatch repair in mtDNA, these processes are still not well characterized.^[159]

Lack of mitochondrial DNA[edit]

Eukaryotic cells typically have mitochondrial DNA; however, mitochondria that lack their own DNA have been found in a marine parasitic dinoflagellate from the genus Amoebophyra. This microorganism, A. cerati, has functional mitochondria that lack a genome.^[164] In related species, the mitochondrial genome still has three genes, but in A. cerati only a single mitochondrial gene — the cytochrome c oxidase I gene (cox1) — is found, and it has migrated to the genome of the nucleus.^[165]

Population genetic studies[edit]

Main article: Human mitochondrial genetics

The near-absence of genetic recombination in mitochondrial DNA makes it a useful source of information for scientists involved in population genetics and evolutionary biology^[166] Because all the mitochondrial DNA is inherited as a single unit, or haplotype, the relationships between mitochondrial DNA from different individuals can be represented as a gene treehuman evolutionary genetics, where the molecular clock can be used to provide a recent date for mitochondrial Eve^[167][168] This is often interpreted as strong support for a recent modern human expansion out of Africa^[169] Another human example is the sequencing of mitochondrial DNA from Neanderthal^[170]

However, mitochondrial DNA reflects only the history of the females in a population and so may not represent the history of the population as a whole. This can be partially overcome by the use of paternal genetic sequences, such as the non-recombining region of the Y-chromosome^[169] In a broader sense, only studies that also include nuclear DNA^[171]

Recent measurements of the molecular clock for mitochondrial DNA^[172] reported a value of 1 mutation every 7884 years dating back to the most recent common ancestor of humans and apes, which is consistent with estimates of mutation rates of autosomal DNA (10⁻⁸ per base per generation.^[173]

Dysfunction and disease[edit]

Mitochondrial diseases[edit]

Main article: Mitochondrial disease

Damage and subsequent dysfunction in mitochondria is an important factor in a range of human diseases due to their influence in cell metabolism. Mitochondrial disorders often present themselves as neurological disorders, including autism^[16] They can also manifest as myopathy, diabetes, multiple endocrinopathy^[174] Diseases caused by mutation in the mtDNA include Kearns–Sayre syndrome, MELAS syndrome and Leber's hereditary optic neuropathy^[175] In the vast majority of cases, these diseases are transmitted by a female to her children, as the zygotePearson syndrome, and progressive external ophthalmoplegiapoint mutations^[174]

In other diseases, defects in nuclear genes lead to dysfunction of mitochondrial proteins. This is the case in Friedreich's ataxia, hereditary spastic paraplegia, and Wilson's disease^[176] These diseases are inherited in a dominance relationshipcoenzyme Q10 deficiency and Barth syndrome^[174] Environmental influences may interact with hereditary predispositions and cause mitochondrial disease. For example, there may be a link between pesticide exposure and the later onset of Parkinson's disease^[177][178] Other pathologies with etiology involving mitochondrial dysfunction include schizophrenia, bipolar disorder, dementia, Alzheimer's disease,^[179] Parkinson's disease, epilepsy, stroke, cardiovascular disease, chronic fatigue syndrome, retinitis pigmentosa, and diabetes mellitus^[180][181]

Mitochondria-mediated oxidative stress plays a role in cardiomyopathy in Type 2 diabetics. Increased fatty acid delivery to the heart increases fatty acid uptake by cardiomyocytes, resulting in increased fatty acid oxidation in these cells. This process increases the reducing equivalents available to the electron transport chain of the mitochondria, ultimately increasing reactive oxygen species (ROS) production. ROS increases uncoupling proteins (UCPs) and potentiate proton leakage through the adenine nucleotide translocator (ANT), the combination of which uncouples^[182]

Possible relationships to aging[edit]

Given the role of mitochondria as the cell's powerhouse, there may be some leakage of the high-energy electrons in the respiratory chain to form reactive oxygen speciesoxidative stress^[183] Hypothesized links between aging and oxidative stress are not new and were proposed in 1956,^[184] which was later refined into the mitochondrial free radical theory of aging^[185] A vicious cycle was thought to occur, as oxidative stress leads to mitochondrial DNA mutations, which can lead to enzymatic abnormalities and further oxidative stress.

A number of changes can occur to mitochondria during the aging process.^[186] Tissues from elderly patients show a decrease in enzymatic activity of the proteins of the respiratory chain.^[187] However, mutated mtDNA can only be found in about 0.2% of very old cells.^[188] Large deletions in the mitochondrial genome have been hypothesized to lead to high levels of oxidative stress and neuronal death in Parkinson's disease^[189]

In popular culture[edit]

Madeleine L'Engle's 1973 science fantasy novel A Wind in the Door prominently features the mitochondria of main character Charles Wallace Murry, as being inhabited by creatures known as the farandolae

The 1995 horror fiction novel Parasite Eve by Hideaki Sena depicts mitochondria as having some consciousness and mind controlfilm, video game, and video game sequel

In the Star Wars franchise, microorganismsthe ForceGeorge Lucas, director of the 1999 film Star Wars: Episode I – The Phantom Menace, in which midi-chlorians were introduced, described them as "a loose depiction of mitochondria".^[190] The non-fictional bacteria genus Midichloria was later named after the midi-chlorians of Star Wars.

As a result of the mitochondrion's prominence in modern American science education, the phrase "the mitochondria is the powerhouse of the cell" became an internet memetRNA^[191][192]

See also[edit]

• Anti-mitochondrial antibodies
• Chloroplast
• Hydrogenosome
• Midichloria bacterial genus
• Mitochondrial metabolic rates
• Mitochondrial permeability transition pore
• Nebenkern
• Oncocyte
• Oncocytoma
• Paternal mtDNA transmission
• Plastid
• Submitochondrial particle
• TIM/TOM complex

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General

•  This article incorporates public domain material from the NCBI document: "Science Primer"

For more info Read the ncert class 8,9,10,11,12

External links[edit]

• Lane, Nick (2016). The Vital Question: Energy, Evolution, and the Origins of Complex Life. WW Norton & Company. ISBN 978-0393352979

Wikimedia Commons has media related to Mitochondrion.

• Mitodb.com
• Mitochondria Atlas at University of Mainz
• Mitochondria Research Portal
• Mitochondria: Architecture dictates function
• Mitochondria links at University of Alabama
• MIP Mitochondrial Physiology Society
• 3D structures of proteins from inner mitochondrial membrane at University of Michigan
• 3D structures of proteins associated with outer mitochondrial membrane at University of Michigan
• Mitochondrial Protein Partnership at University of Wisconsin
• MitoMiner – A mitochondrial proteomics database at MRC Mitochondrial Biology Unit
• Mitochondrion – Cell Centered Database
• Mitochondrion Reconstructed by Electron Tomography at San Diego State University
• Video Clip of Rat-liver Mitochondrion from Cryo-electron Tomography

Mitochondrial Diversity.

show v t e Structures of the cell / organelles
Endomembrane system	Cell membrane Nucleus Endoplasmic reticulum Golgi apparatus Parenthesome Autophagosome Vesicle Exosome Lysosome Endosome Phagosome Vacuole Acrosome Cytoplasmic granule Melanosome Microbody Glyoxysome Peroxisome Weibel–Palade body
Cytoskeleton	Microfilament Intermediate filament Microtubule Prokaryotic cytoskeleton Microtubule organizing center Centrosome Centriole Basal body Spindle pole body Myofibril
Endosymbionts	Mitochondrion Plastid Chloroplast Chromoplast Gerontoplast Leucoplast Amyloplast Elaioplast Proteinoplast Tannosome
Other internal	Nucleolus RNA Ribosome Spliceosome Vault Cytoplasm Cytosol Inclusions Proteasome
External	Undulipodium Cilium Flagellum Axoneme Radial spoke Archaellum Cell wall Extracellular matrix

show

• v
• t
• e

Mitochondrial proteins

Outer membrane

fatty acid degradation	Carnitine palmitoyltransferase I Long-chain-fatty-acid—CoA ligase
tryptophan metabolism	Kynureninase
monoamine neurotransmitter metabolism	Monoamine oxidase

Intermembrane space

• Adenylate kinase
• Creatine kinase

Inner membrane

oxidative phosphorylation	Coenzyme Q – cytochrome c reductase Cytochrome c NADH dehydrogenase Succinate dehydrogenase
pyrimidine metabolism	Dihydroorotate dehydrogenase
mitochondrial shuttle	Malate-aspartate shuttle Glycerol phosphate shuttle
steroidogenesis	Cholesterol side-chain cleavage enzyme Steroid 11-beta-hydroxylase Aldosterone synthase
other	Glutamate aspartate transporter Glycerol-3-phosphate dehydrogenase ATP synthase Carnitine palmitoyltransferase II Uncoupling protein

Matrix

citric acid cycle	Citrate synthase Aconitase Isocitrate dehydrogenase Oxoglutarate dehydrogenase complex Succinyl coenzyme A synthetase Fumarase Malate dehydrogenase
anaplerotic reactions	Aspartate transaminase Glutamate dehydrogenase Pyruvate dehydrogenase complex
urea cycle	Carbamoyl phosphate synthetase I Ornithine transcarbamylase N-Acetylglutamate synthase
alcohol metabolism	ALDH2
PMPCB

Other/to be sorted

• Frataxin
• Mitochondrial membrane transport protein
  • Mitochondrial permeability transition pore
  • Mitochondrial carrier

Mitochondrial DNA

Complex I	MT-ND1 MT-ND2 MT-ND3 MT-ND4 MT-ND4L MT-ND5 MT-ND6
Complex III	MT-CYB
Complex IV	MT-CO1 MT-CO2 MT-CO3
ATP synthase	MT-ATP6 MT-ATP8
tRNA	MT-TA MT-TC MT-TD MT-TE MT-TF MT-TG MT-TH MT-TI MT-TK MT-TL1 MT-TL2 MT-TM MT-TN MT-TP MT-TQ MT-TR MT-TS1 MT-TS2 MT-TT MT-TV MT-TW MT-TY

see also mitochondrial diseases

Authority control	BNE: XX535796 BNF: cb12175492v (data) GND: 4124939-2 LCCN: sh85086280 NDL: 00567726

Retrieved from "https://en.wikipedia.org/w/index.php?title=Mitochondrion&oldid=947812300"

Categories:

• Mitochondria
• Cellular respiration
• Endosymbiotic events