The CcmC-CcmE interaction during cytochrome c maturation by System I is driven by protein-protein and not protein-heme contacts.

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26 octobre 2018

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Périmètre
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Serveur académique Lausannois

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Ce document est lié à :
info:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.RA118.005024

Ce document est lié à :
info:eu-repo/semantics/altIdentifier/pmid/30206118

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info:eu-repo/semantics/altIdentifier/eissn/1083-351X

Ce document est lié à :
info:eu-repo/semantics/altIdentifier/urn/urn:nbn:ch:serval-BIB_438639CA14171

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Serveur Académique Lausannois

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Université de Lausanne et CHUV

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info:eu-repo/semantics/openAccess , Copying allowed only for non-profit organizations , https://serval.unil.ch/disclaimer

Mots-clés 0

Amino Acid Substitution; Apoproteins/chemistry; Apoproteins/genetics; Apoproteins/metabolism; Bacterial Outer Membrane Proteins/chemistry; Bacterial Outer Membrane Proteins/genetics; Bacterial Outer Membrane Proteins/metabolism; Binding Sites; Crystallography, X-Ray; Cytochromes c/chemistry; Cytochromes c/genetics; Cytochromes c/metabolism; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Heme/chemistry; Heme/genetics; Heme/metabolism; Hemeproteins/chemistry; Hemeproteins/genetics; Hemeproteins/metabolism; Membrane Proteins/chemistry; Membrane Proteins/genetics; Membrane Proteins/metabolism; Mutagenesis, Site-Directed; Protein Conformation; Protein Interaction Domains and Motifs; CcmC; CcmE; Gram-negative bacteria; System I; cytochrome c; cytochrome c maturation; heme; nuclear magnetic resonance (NMR); post-translational modification (PTM); protein-protein interactions

Sujets proches En

Hematin E. coli (Bacterium)

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S.H. Shevket et al., « The CcmC-CcmE interaction during cytochrome c maturation by System I is driven by protein-protein and not protein-heme contacts. », Serveur académique Lausannois, ID : 10.1074/jbc.RA118.005024

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Cytochromes c are ubiquitous proteins, essential for life in most organisms. Their distinctive characteristic is the covalent attachment of heme to their polypeptide chain. This post-translational modification is performed by a dedicated protein system, which in many Gram-negative bacteria and plant mitochondria is a nine-protein apparatus (CcmA-I) called System I. Despite decades of study, mechanistic understanding of the protein-protein interactions in this highly complex maturation machinery is still lacking. Here, we focused on the interaction of CcmC, the protein that sources the heme cofactor, with CcmE, the pivotal component of System I responsible for the transfer of the heme to the apocytochrome. Using in silico analyses, we identified a putative interaction site between these two proteins (residues Asp 47 , Gln 50 , and Arg 55 on CcmC; Arg 73 , Asp 101 , and Glu 105 on CcmE), and we validated our findings by in vivo experiments in Escherichia coli Moreover, employing NMR spectroscopy, we examined whether a heme-binding site on CcmE contributes to this interaction and found that CcmC and CcmE associate via protein-protein rather than protein-heme contacts. The combination of in vivo site-directed mutagenesis studies and high-resolution structural techniques enabled us to determine at the residue level the mechanism for the formation of one of the key protein complexes for cytochrome c maturation by System I.

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