Wheat mitochondria ccmB encodes the membrane domain of a putative ABC transporter involved in cytochrome c biogenesis

Faivre-Nitschke, Sandrine Emmanuelle; Nazoa, Patricia; Gualberto, José M.; Grienenberger, Jean‐Michel; Bonnard, Géraldine

doi:10.1016/s0167-4781(01)00239-1

Cited by 25 publications

(10 citation statements)

References 63 publications

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“…Residue H108 of S. putrefaciens CcmB is highly conserved among alpha-, beta-and gammaproteobacteria ( Fig. 2) and is one of six CcmB residues strictly conserved among several land plant mitochondrial orthologs such as those found in Marchantia polymorpha, Arabidopsis thaliana, Triticum aestivum, and Oenothera berteriana and in the red alga Cyanidioschyzon merolae (20). Respiratory mutant CCMB1 retains the ability to respire on electron acceptors with high (but not low) reduction potentials (E 0 ).…”

Section: Resultsmentioning

confidence: 99%

A Conserved Histidine in Cytochrome c Maturation Permease CcmB of Shewanella putrefaciens Is Required for Anaerobic Growth below a Threshold Standard Redox Potential

2007

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. Genetic complementation and nucleotide sequence analyses indicated that the CCMB1 respiratory mutant phenotype was due to mutation of a conserved histidine residue (H108Y) in a protein that displayed high homology to Escherichia coli CcmB, the permease subunit of an ABC transporter involved in cytochrome c maturation. Although CCMB1 retained the ability to grow on electron acceptors with high E 0 , the cytochrome content of CCMB1 was <10% of that of the wild-type strain. Periplasmic extracts of CCMB1 contained slightly greater concentrations of the thiol functional group (-SH) than did the wild-type strain, an indication that the E h of the CCMB1 periplasm was abnormally low. A ccmB deletion mutant was unable to respire anaerobically on any electron acceptor, yet retained aerobic respiratory capability. These results suggest that the mutation of a conserved histidine residue (H108) in CCMB1 alters the redox homeostasis of the periplasm during anaerobic growth on electron acceptors with low (but not high) E 0 . This is the first report of the effects of Ccm deficiencies on bacterial respiration of electron acceptors whose E 0 nearly span the entire redox continuum.

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Section: Resultsmentioning

confidence: 99%

A Conserved Histidine in Cytochrome c Maturation Permease CcmB of Shewanella putrefaciens Is Required for Anaerobic Growth below a Threshold Standard Redox Potential

2007

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“…Functional complementation of an E. coli mutant lacking CcmE with its A. thaliana counterpart, and related protein interaction studies, indicated that the mitochondrial CcmE binds heme b via a conserved His residue, and that CcmABC form an ABC-type transporter with ATP hydrolysis activity [49, 75, 76]. …”

Section: Ccm-system I: Functional Organizationmentioning

confidence: 99%

Cytochrome c biogenesis System I: An intricate process catalyzed by a maturase supercomplex?

Verissimo

Daldal

2014

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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Cytochromes c are ubiquitous heme proteins that are found in most living organisms and are essential for various energy production pathways as well as other cellular processes. Their biosynthesis relies on a complex post-translational process, called cytochrome c biogenesis, responsible for the formation of stereo-specific thioether bonds between the vinyl groups of heme b (protoporphyrin IX-Fe) and the thiol groups of apocytochromes c heme-binding site (C1XXC2H) cysteine residues. In some organisms this process involves up to nine (CcmABCDEFGHI) membrane proteins working together to achieve heme ligation, designated the Cytochrome c maturation (Ccm)-System I. Here, we review recent findings related to the Ccm-System I found in bacteria, archaea and plant mitochondria, with an emphasis on protein interactions between the Ccm components and their substrates (apocytochrome c and heme). We discuss the possibility that the Ccm proteins may form a multi subunit supercomplex (dubbed “Ccm machine”), and based on the currently available data, we present an updated version of a mechanistic model for Ccm.

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“…In addition translation of ccm genes was shown for some wheat proteins, i.e. for CcmB [15] and for CcmF N [16], a protein similar to the N‐terminal part of the bacterial protein CcmF [17]. The protein described here, CcmF C , is similar to the C‐terminal region of CcmF.…”

Section: Introductionmentioning

confidence: 61%

“…[7]. In wheat particularly, three open reading frames of 206 ( ccmB ) [15], 240 ( ccmC ) [19] and 575 ( ccmF N ) [16] codons were found. The latter gene encodes a protein homologous to the N‐terminal part of the bacterial CcmF [17].…”

Section: Resultsmentioning

confidence: 97%

“…A possible cytochrome c assembly complex taking into account a A 2 B 2 CEF N F C H stoichiometry, with the calculated sizes of the identified CCM gene products in plant mitochondria, i.e. 28 kDa for CCMA (N. Rayapuram, unpublished data), 22 kDa for CcmB [15], 27 kDa for CcmC [19], 65 kDa for CcmF N [16], 50 kDa for CcmF C , 27 kDa for CCME [8] and 20 kDa for CCMH (E. Meyer, unpublished data) would make a total of 289 kDa. This is still some way short of the observed complex of 700 kDa.…”

Section: Resultsmentioning

confidence: 99%

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CcmF_C involved in cytochrome c maturation is present in a large sized complex in wheat mitochondria

et al. 2004

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In land plant mitochondria, c-type cytochromes are assembled via a mechanism similar to that found in Gram-negative bacteria and di¡erent from that used by mitochondria from other eukaryotes. The wheat mitochondrial genome encodes CCM (for cytochrome c maturation) proteins, among them CcmF C , a protein similar to the C-terminal part of the bacterial CcmF. The gene is transcribed into a 1.7 kb transcript at steady state. However, the 3P P termini of the transcript were found to occur upstream of the deduced gene termination codon. This discrepancy was solved by RNA editing that introduces a novel termination codon, thus shortening the reading frame by 27 codons. The processed transcript is translated into a protein integrated in the mitochondrial inner membrane. We also show that the protein is part of a large (700 kDa) protein complex, that possibly represents a cytochrome c assembly complex. ß 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.

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Wheat mitochondria ccmB encodes the membrane domain of a putative ABC transporter involved in cytochrome c biogenesis

Cited by 25 publications

References 63 publications

A Conserved Histidine in Cytochrome c Maturation Permease CcmB of Shewanella putrefaciens Is Required for Anaerobic Growth below a Threshold Standard Redox Potential

A Conserved Histidine in Cytochrome c Maturation Permease CcmB of Shewanella putrefaciens Is Required for Anaerobic Growth below a Threshold Standard Redox Potential

Cytochrome c biogenesis System I: An intricate process catalyzed by a maturase supercomplex?

CcmF_C involved in cytochrome c maturation is present in a large sized complex in wheat mitochondria

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Wheat mitochondria ccmB encodes the membrane domain of a putative ABC transporter involved in cytochrome c biogenesis

Cited by 25 publications

References 63 publications

A Conserved Histidine in Cytochrome c Maturation Permease CcmB of Shewanella putrefaciens Is Required for Anaerobic Growth below a Threshold Standard Redox Potential

A Conserved Histidine in Cytochrome c Maturation Permease CcmB of Shewanella putrefaciens Is Required for Anaerobic Growth below a Threshold Standard Redox Potential

Cytochrome c biogenesis System I: An intricate process catalyzed by a maturase supercomplex?

CcmFC involved in cytochrome c maturation is present in a large sized complex in wheat mitochondria

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CcmF_C involved in cytochrome c maturation is present in a large sized complex in wheat mitochondria