Biogenesis and assembly of eukaryotic cytochrome c oxidase catalytic core

Soto, Ileana; Fontanesi, Flavia; Liu, Jingjing; Barrientos, Antoni

doi:10.1016/j.bbabio.2011.09.005

Cited by 195 publications

(218 citation statements)

References 203 publications

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“…COX I and COX II are the two copper-containing subunits harboring the Cu B and Cu A sites, respectively, conserved in heme-copper oxidases (7)(8)(9). Assembly of the oxidase is a complex process involving the synthesis and folding of the individual subunits and the incorporation of the metal cofactors (10). For the human oxidase, at least seven genes encoding for different proteins are required for maturation of these two copper sites (11)(12)(13)(14)(15)(16)(17).…”

Section: Sco Proteinsmentioning

confidence: 99%

Loop recognition and copper-mediated disulfide reduction underpin metal site assembly of Cu _A in human cytochrome oxidase

Morgada

Abriata

Cefaro

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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Maturation of cytochrome oxidases is a complex process requiring assembly of several subunits and adequate uptake of the metal cofactors. Two orthologous Sco proteins (Sco1 and Sco2) are essential for the correct assembly of the dicopper Cu A site in the human oxidase, but their function is not fully understood. Here, we report an in vitro biochemical study that shows that Sco1 is a metallochaperone that selectively transfers Cu(I) ions based on loop recognition, whereas Sco2 is a copper-dependent thiol reductase of the cysteine ligands in the oxidase. Copper binding to Sco2 is essential to elicit its redox function and as a guardian of the reduced state of its own cysteine residues in the oxidizing environment of the mitochondrial intermembrane space (IMS). These results provide a detailed molecular mechanism for Cu A assembly, suggesting that copper and redox homeostasis are intimately linked in the mitochondrion.

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Section: Sco Proteinsmentioning

confidence: 99%

Loop recognition and copper-mediated disulfide reduction underpin metal site assembly of Cu _A in human cytochrome oxidase

Morgada

Abriata

Cefaro

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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“…1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 61 62 63 64 65 16 [17], (c) [68], (d) [69], (e) [70], (f) [71], (g) [72], (h) [73], (i) [74], (j) [75], (k) [76], (l) [77], (m) [22], (n) [29], (o) [78], (p) [58], (q) [79], (r)[34] 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 61 62 63 64 65 17 ((a) [48], (b) [45], (c) [47], (d) [43], (e) [44], (f) [39], (g) …”

Section: Resultsunclassified

Respiratory-deficient mutants of the unicellular green alga Chlamydomonas: A review

et al. 2014

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Genetic manipulation of the unicellular green alga Chlamydomonas reinhardtii is straightforward. Nuclear genes can be interrupted by insertional mutagenesis or targeted by RNA interference whereas random or site-directed mutagenesis allows the introduction of mutations in the mitochondrial genome. This, combined with a screen that easily allows discriminating respiratorydeficient mutants, makes Chlamydomonas a model system of choice to study mitochondria biology in photosynthetic organisms. Since the first description of Chlamydomonas respiratory-deficient mutants in 1977 by random mutagenesis, many other mutants affected in mitochondrial components have been characterized. These respiratory-deficient mutants increased our knowledge on function and assembly of the respiratory enzyme complexes. More recently some of these mutants allowed the study of mitochondrial gene expression processes poorly understood in Chlamydomonas. In this review, we update the data concerning the respiratory components with a special focus on the assembly factors identified on other organisms. In addition, we make an inventory of different mitochondrial respiratory mutants that are inactivated either on mitochondrial or nuclear genes. Opposed Reviewers:Claire Remacle -Génétique des microorganismes -Institut de Botanique B22 Boulevard du Rectorat, 27 -Université de Liège-B-4000 Liège, Belgique Tel +32 4 3663812 -Fax +32 4 3663840 e-mail: c.remacle@ulg.ac.be First, we wish to thank the two anonymous reviewers for their constructive comments. We found their suggestions very helpful to improve the quality of our manuscript. We have addressed all the points they raised and have modified the text accordingly. A detailed response to reviewers' comments is included below.We believe we have addressed all referees' comments and we hope this revised version is now suitable for publication in Biochimie.We are looking forward to hearing from you, With best regards, Cover LetterResponse to reviewers The text has been modified in order to give more background details on the methodology used to create and screen respiratory mutants in Chlamydomonas. The main modifications correspond to: Paragraph 2.3: -p8. A figure (Fig. 4) has been added in order to provide more information on dark-dier/slow growth screens for different classes of mutant.-p9. The mitochondrial transformation method used in Chlamydomonas has been detailed.Paragraph 2.4: -p10. The TTC-based screen has been explained.Finally, all along the text the methods used to create nuclear and mitochondrial mutants has been indicated. Also, the text could benefit from being proof-read by a native English speaker as the grammar is a little awkward in places. I highlight a couple of points below, but there are a number of other places where the English could be improved for clarity.The text has been proof-read by a good English speaker as requested and the text has been modified according to the comments.Minor points:1. Abstract, line 1: "the genetics" have been replaced by "genetic manipu...

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“…Because the effect of Pet54 on the COX1 5Ј-UTR was observable only in the presence of the Cox1 protein, there was a possibility that Pet54 could affect either Mss51 or the COA complexes. COA complexes depend on the presence of Cox1 protein, and Mss51 activity in translation activation depends on how much of this activator is released from the COA complexes (1,15,19,21). Therefore, we first analyzed by BN-PAGE whether Mss51 and Pet54 co-migrate.…”

Section: Pet54 Could Promote Mss51mentioning

confidence: 99%

A Novel Function of Pet54 in Regulation of Cox1 Synthesis in Saccharomyces cerevisiae Mitochondria

Mayorga

Camacho‐Villasana

Shingú-Vázquez

et al. 2016

Journal of Biological Chemistry

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Cytochrome c oxidase assembly requires the synthesis of the mitochondria-encoded core subunits, Cox1, Cox2, and Cox3. In yeast, Pet54 protein is required to activate translation of the COX3 mRNA and to process the aI5␤ intron on the COX1 transcript. Here we report a third, novel function of Pet54 on Cox1 synthesis. We observed that Pet54 is necessary to achieve an efficient Cox1 synthesis. Translation of the COX1 mRNA is coupled to the assembly of cytochrome c oxidase by a mechanism that involves Mss51. This protein activates translation of the COX1 mRNA by acting on the COX1 5-UTR, and, in addition, it interacts with the newly synthesized Cox1 protein in high molecular weight complexes that include the factors Coa3 and Cox14. Deletion of Pet54 decreased Cox1 synthesis, and, in contrast to what is commonly observed for other assembly mutants, double deletion of cox14 or coa3 did not recover Cox1 synthesis. Our results show that Pet54 is a positive regulator of Cox1 synthesis that renders Mss51 competent as a translational activator of the COX1 mRNA and that this role is independent of the assembly feedback regulatory loop of Cox1 synthesis. Pet54 may play a role in Mss51 hemylation/conformational change necessary for translational activity. Moreover, Pet54 physically interacts with the COX1 mRNA, and this binding was independent of the presence of Mss51.Cytochrome c oxidase (CcO) 3 is the last electron acceptor of the mitochondrial respiratory chain. In the yeast Saccharomyces cerevisiae, this enzyme contains 12 subunits, three of which (Cox1, Cox2, and Cox3) are encoded by the mitochondrial DNA. Assembly of CcO is a complex process regulated by more than 25 factors and chaperones (for reviews, see Ref. 1). The first steps of CcO biogenesis involve the translational activation of the mitochondria-encoded mRNAs COX1, COX2, and COX3 by mRNA-specific proteins. Translational activation of the COX1 mRNA depends on Pet309 and Mss51 (2, 3), whereas COX2 translation depends on Pet111 (4, 5), and COX3 mRNA translation depends on Pet54, Pet122, and Pet494 (6 -9). These proteins act on the target mRNA 5Ј-UTRs to allow translation by the mitochondrial ribosomes. They interact with each other and with the mitochondrial inner membrane and are thought to tether translation initiation close to the assembly sites of CcO in the membrane (for a review, see Ref. 10) (11). The mitochondria-encoded Cox1, Cox2, and Cox3 subunits are proposed to assemble from three different modules, each containing a specific subset of nucleus-encoded subunits (12-14).Cox1, the largest subunit of the CcO, carries the heme aa 3 -Cu B center to reduce oxygen. Synthesis of Cox1 inside mitochondria is highly regulated. If CcO assembly is blocked by mutations on either integral subunits or accessory chaperones, Cox1 synthesis is down-regulated (15, 16). It is proposed that by this mechanism, mitochondria avoids accumulation of pro-oxidant Cox1 intermediates (17). In addition to its role as translational activator of COX1 mRNA, Mss51 also physically inter...

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Biogenesis and assembly of eukaryotic cytochrome c oxidase catalytic core

Cited by 195 publications

References 203 publications

Loop recognition and copper-mediated disulfide reduction underpin metal site assembly of Cu _A in human cytochrome oxidase

Loop recognition and copper-mediated disulfide reduction underpin metal site assembly of Cu _A in human cytochrome oxidase

Respiratory-deficient mutants of the unicellular green alga Chlamydomonas: A review

A Novel Function of Pet54 in Regulation of Cox1 Synthesis in Saccharomyces cerevisiae Mitochondria

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Biogenesis and assembly of eukaryotic cytochrome c oxidase catalytic core

Cited by 195 publications

References 203 publications

Loop recognition and copper-mediated disulfide reduction underpin metal site assembly of Cu A in human cytochrome oxidase

Loop recognition and copper-mediated disulfide reduction underpin metal site assembly of Cu A in human cytochrome oxidase

Respiratory-deficient mutants of the unicellular green alga Chlamydomonas: A review

A Novel Function of Pet54 in Regulation of Cox1 Synthesis in Saccharomyces cerevisiae Mitochondria

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Loop recognition and copper-mediated disulfide reduction underpin metal site assembly of Cu _A in human cytochrome oxidase

Loop recognition and copper-mediated disulfide reduction underpin metal site assembly of Cu _A in human cytochrome oxidase