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The interplay between the disulfide bond formation pathway and cytochrome c maturation in Escherichia coli
Author(s) -
Mavridou Despoina A.I.,
Ferguson Stuart J.,
Stevens Julie M.
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.04.055
Subject(s) - dsba , periplasmic space , biogenesis , escherichia coli , heme , context (archaeology) , biochemistry , chemistry , hemeprotein , cysteine , cytochrome , cytochrome c , disulfide bond , biology , enzyme , mitochondrion , gene , paleontology
Heme attachment to c ‐type cytochromes in bacteria requires cysteine thiols in the CXXCH motif of the protein. The involvement of the periplasmic disulfide generation system in this process remains unclear. We undertake a systematic evaluation of the role of DsbA and DsbD in cytochrome c biogenesis in Escherichia coli and show unequivocally that DsbA is not essential for holocytochrome production under aerobic or anaerobic conditions. We also prove that DsbD is important but not essential for maturation of c ‐type cytochromes. We discuss the findings in the context of a model in which heme attachment to, and oxidation of, the apocytochrome are competing processes.