Mitochondrial cytochrome c oxidase biogenesis: Recent developments

Timón‐Gómez, Alba; Nývltová, Eva; Abriata, Luciano A.; Vila, Alejandro J.; Hosler, Jonathan P.; Barrientos, Antoni

doi:10.1016/j.semcdb.2017.08.055

Cited by 284 publications

(270 citation statements)

References 126 publications

(216 reference statements)

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“…Based on in silico data, MITRAC15 has been suggested to represent a homologue of the S. cerevisiae COA1, a protein that participates in complex IV biogenesis [3,4,9]. Based on in silico data, MITRAC15 has been suggested to represent a homologue of the S. cerevisiae COA1, a protein that participates in complex IV biogenesis [3,4,9].…”

Section: Resultsmentioning

confidence: 99%

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MITRAC15/COA1 promotes mitochondrial translation in a ND2 ribosome–nascent chain complex

et al. 2019

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The mitochondrial genome encodes for thirteen core subunits of the oxidative phosphorylation system. These proteins assemble with imported proteins in a modular manner into stoichiometric enzyme complexes. Assembly factors assist in these biogenesis processes by providing co-factors or stabilizing transient assembly stages. However, how expression of the mitochondrial-encoded subunits is regulated to match the availability of nuclear-encoded subunits is still unresolved. Here, we address the function of MITRAC15/COA1, a protein that participates in complex I biogenesis and complex IV biogenesis. Our analyses of a MITRAC15 knockout mutant reveal that MITRAC15 is required for translation of the mitochondrial-encoded complex I subunit ND2. We find that MITRAC15 is a constituent of a ribosome-nascent chain complex during ND2 translation. Chemical crosslinking analyses demonstrate that binding of the ND2-specific assembly factor ACAD9 to the ND2 polypeptide occurs at the C-terminus and thus downstream of MITRAC15. Our analyses demonstrate that expression of the founder subunit ND2 of complex I undergoes regulation. Moreover, a ribosome-nascent chain complex with MITRAC15 is at the heart of this process.

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Section: Resultsmentioning

confidence: 99%

“…These assembly factors represent a functionally heterogeneous group of proteins that fulfill different and mostly complexspecific functions [7][8][9][10]. These assembly factors represent a functionally heterogeneous group of proteins that fulfill different and mostly complexspecific functions [7][8][9][10].…”

Section: Introductionmentioning

confidence: 99%

MITRAC15/COA1 promotes mitochondrial translation in a ND2 ribosome–nascent chain complex

et al. 2019

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“…(Table ), and we will discuss similarities and differences with the B. diazoefficiens system. The current status of Cu A biosynthesis in eukaryotic mitochondria was treated competently in two recently published review articles . We feel there is no need to recapitulate those conclusions here, except on few occasions.…”

Section: Bacterial Species Investigated For the Presence Of Tlpa‐ Scmentioning

confidence: 89%

“…Since then, a large body of literature was published with the undisputed consensus that members of the Sco protein family are functionally linked with the synthesis of the Cu A center in subunit II of cytochrome c oxidase (for reviews, see refs. ). A large majority (approx.…”

Section: Portrayal Of Three Key Players In the Formation Of Active Cymentioning

confidence: 97%

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Biochemical pathway for the biosynthesis of the Cu_A center in bacterial cytochrome c oxidase

2019

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The di‐copper center CuA is an essential metal cofactor in cytochrome oxidase (Cox) of mitochondria and many prokaryotes, mediating one‐electron transfer from cytochrome c to the site for oxygen reduction. CuA is located in subunit II (CoxB) of Cox and protrudes into the periplasm of Gram‐negative bacteria or the mitochondrial intermembrane space. How the two copper ions are brought together to build CoxB·CuA is the subject of this review. It had been known that the reductase TlpA and the metallochaperones ScoI and PcuC are required for CuA formation in bacteria, but the mechanism of copper transfer has emerged only recently for the Bradyrhizobium diazoefficiens system. It consists of the following steps: (a) TlpA keeps the active site cysteine pair of CoxB in its dithiol state as a prerequisite for metal insertion; (b) ScoI·Cu2+ rapidly forms a transient complex with apo‐CoxB; (c) PcuC, loaded with Cu1+ and Cu2+, dissociates this complex to CoxB·Cu2+, and a second PcuC·Cu1+·Cu2+ transfers Cu1+ to CoxB·Cu2+, yielding mature CoxB·CuA. Variants of this pathway might exist in other bacteria or mitochondria.

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Mitochondrial disorders of the OXPHOS system

2020

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Mitochondrial disorders are amongst the most frequent inborn errors of metabolism, their primary cause being the dysfunction of the oxidative phosphorylation system (OXPHOS). OXPHOS is composed of the electron transport chain (ETC), formed by four multimeric enzymes and two mobile electron carriers, plus an ATP synthase (also called complex V). The ETC performs the redox reactions involved in cellular respiration while generating the proton motive force used by complex V to synthesize ATP. OXPHOS biogenesis involves multiple steps, starting from the expression of genes encoded in physically separated genomes, namely the mitochondrial and nuclear DNA, to the coordinated assembly of components and cofactors building each individual complex and eventually the supercomplexes. The genetic cause underlying around half of the diagnosed mitochondrial disease cases is currently known. Many of these cases result from pathogenic variants in genes encoding structural subunits or additional factors directly involved in the assembly of the ETC complexes. Here we review the historical and most recent findings concerning the clinical phenotypes and the molecular pathological mechanisms underlying this particular group of disorders.

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Mitochondrial cytochrome c oxidase biogenesis: Recent developments

Cited by 284 publications

References 126 publications

MITRAC15/COA1 promotes mitochondrial translation in a ND2 ribosome–nascent chain complex

MITRAC15/COA1 promotes mitochondrial translation in a ND2 ribosome–nascent chain complex

Biochemical pathway for the biosynthesis of the Cu_A center in bacterial cytochrome c oxidase

Mitochondrial disorders of the OXPHOS system

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Mitochondrial cytochrome c oxidase biogenesis: Recent developments

Cited by 284 publications

References 126 publications

MITRAC15/COA1 promotes mitochondrial translation in a ND2 ribosome–nascent chain complex

MITRAC15/COA1 promotes mitochondrial translation in a ND2 ribosome–nascent chain complex

Biochemical pathway for the biosynthesis of the CuA center in bacterial cytochrome c oxidase

Mitochondrial disorders of the OXPHOS system

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Product

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Biochemical pathway for the biosynthesis of the Cu_A center in bacterial cytochrome c oxidase