ArticleThe Biochemical journal2001
The Escherichia coli CcmG protein fulfils a specific role in cytochrome c assembly.
Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 68 citations in OpenAlex.
- From genes to function: regulation, maturation, and evolution of cytochromeApplied and environmental microbiology · 2025Review
- An Archaea-specificeLife · 2022Article
- Pathways of Iron and Sulfur Acquisition, Cofactor Assembly, Destination, and Storage in Diverse Archaeal Methanogens and Alkanotrophs.Journal of bacteriology · 2021Article
- The thioreduction component CcmG confers efficiency and the heme ligation component CcmH ensures stereo-specificity during cytochromeThe Journal of biological chemistry · 2017Article
- Disulfide-Bond-Forming Pathways in Gram-Positive Bacteria.Journal of bacteriology · 2015Review
- Cytochrome c biogenesis System I: an intricate process catalyzed by a maturase supercomplex?Biochimica et biophysica acta · 2014Review
- An extended active-site motif controls the reactivity of the thioredoxin fold.The Journal of biological chemistry · 2014Article
- Structure analysis of the extracellular domain reveals disulfide bond forming-protein properties of Mycobacterium tuberculosis Rv2969c.Protein & cell · 2013Article
- Comparative genomics of Salmonella enterica serovars Derby and Mbandaka, two prevalent serovars associated with different livestock species in the UK.BMC genomics · 2013Article
- Protein Machineries Involved in the Attachment of Heme to Cytochrome c: Protein Structures and Molecular Mechanisms.Scientifica · 2013Review
- 1H, 13C and 15N resonance assignments for the oxidized and reduced states of the N-terminal domain of DsbD from Escherichia coli.Biomolecular NMR assignments · 2012Article
- A comparison of the endotoxin biosynthesis and protein oxidation pathways in the biogenesis of the outer membrane of Escherichia coli and Neisseria meningitidis.Frontiers in cellular and infection microbiology · 2012Review
- Thiol/Disulfide system plays a crucial role in redox protection in the acidophilic iron-oxidizing bacterium Leptospirillum ferriphilum.PloS one · 2012Article
- Cytochrome c biogenesis System I.The FEBS journal · 2011Review
- Detection and function of an intramolecular disulfide bond in the pH-responsive CadC of Escherichia coli.BMC microbiology · 2011Article
- Cytochrome c biogenesis: the Ccm system.Trends in microbiology · 2010Review
- An extracellular disulfide bond forming protein (DsbF) from Mycobacterium tuberculosis: structural, biochemical, and gene expression analysis.Journal of molecular biology · 2010Article
- Disulfide bond formation and cysteine exclusion in gram-positive bacteria.The Journal of biological chemistry · 2010Article
- A periplasmic thioredoxin-like protein plays a role in defense against oxidative stress in Neisseria gonorrhoeae.Infection and immunity · 2009Article
- DSB proteins and bacterial pathogenicity.Nature reviews. Microbiology · 2009Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Escherichia coli K-12, c-type cytochromes are synthesized only during anaerobic growth with trimethylamine-N-oxide, nitrite or low concentrations of nitrate as the terminal electron acceptor. A thioredoxin-like protein, CcmG, is one of 12 proteins required for their assembly in the periplasm. Its postulated function is to reduce disulphide bonds formed between correctly paired cysteine residues in the cytochrome c apoproteins prior to haem attachment by CcmF and CcmH. We report that loss of CcmG synthesis by mutation was not compensated by a second mutation in disulphide-bond-forming proteins, DsbA or DsbB, or by the chemical reductant, 2-mercaptoethanesulphonic acid. An anti-CcmG polyclonal antibody was used in Western-blot analysis to probe the redox state of CcmG in mutants defective in the synthesis of other proteins essential for cytochrome c assembly. The oxidized form of CcmG accumulated not only in trxA or dipZ mutants defective in the transfer of electrons from the cytoplasm for disulphide isomerization and reduction reactions in the periplasm, but also in ccmF and ccmH mutants. The requirement of both CcmF and CcmH for the reduction of the disulphide bond in CcmG indicates that CcmG functions later than CcmF and CcmH in cytochrome c assembly, rather than in electron transfer from the membrane-associated DipZ (also known as DsbD) to CcmH. The data support a model proposed by others in which CcmG catalyses one of the last reactions specific to cytochrome c assembly.
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