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Bacillus subtilis ResA is a thiol-disulfide oxidoreductase involved in cytochrome c synthesis

Erlendsson, Lydur LU ; Acheson, Richard M.; Hederstedt, Lars LU and Le Brun, Nick E. (2003) In Journal of Biological Chemistry 278(20). p.17852-17858
Abstract
Covalent attachment of heme to apocytochromes c in bacteria occurs on the outside of the cytoplasmic membrane and requires two reduced cysteinyls at the heme binding site. A constructed ResA-deficient Bacillus subtilis strain was found to lack c-type cytochromes. Cytochrome c synthesis was restored in the mutant by: (i) in trans expression of resA; (ii) deficiency in BdbD, a thioldisulfide oxidoreductase that catalyzes formation of an intramolecular disulfide bond in apocytochrome c after transfer of the polypeptide across the cytoplasmic membrane; or (iii) by addition of the reductant dithiothreitol to the growth medium. In vivo studies of ResA showed that it is membrane-associated with its thioredoxin-like domain on the outside of the... (More)
Covalent attachment of heme to apocytochromes c in bacteria occurs on the outside of the cytoplasmic membrane and requires two reduced cysteinyls at the heme binding site. A constructed ResA-deficient Bacillus subtilis strain was found to lack c-type cytochromes. Cytochrome c synthesis was restored in the mutant by: (i) in trans expression of resA; (ii) deficiency in BdbD, a thioldisulfide oxidoreductase that catalyzes formation of an intramolecular disulfide bond in apocytochrome c after transfer of the polypeptide across the cytoplasmic membrane; or (iii) by addition of the reductant dithiothreitol to the growth medium. In vivo studies of ResA showed that it is membrane-associated with its thioredoxin-like domain on the outside of the cytoplasmic membrane. Analysis of a soluble form of the protein revealed two redox reactive cysteine residues with a midpoint potential of about -340 mV at pH 7. We conclude that ResA, probably together with another thiol-disulfide oxidoreductase, CcdA, is required for the reduction of the cysteinyls in the heme binding site of apocytochrome c. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
278
issue
20
pages
17852 - 17858
publisher
ASBMB
external identifiers
  • wos:000182838300034
  • scopus:0038381449
ISSN
1083-351X
DOI
10.1074/jbc.M300103200
language
English
LU publication?
yes
id
561ecfdd-c947-456d-999e-05a3ee74a909 (old id 310877)
date added to LUP
2007-08-29 15:44:11
date last changed
2018-01-07 05:34:54
@article{561ecfdd-c947-456d-999e-05a3ee74a909,
  abstract     = {Covalent attachment of heme to apocytochromes c in bacteria occurs on the outside of the cytoplasmic membrane and requires two reduced cysteinyls at the heme binding site. A constructed ResA-deficient Bacillus subtilis strain was found to lack c-type cytochromes. Cytochrome c synthesis was restored in the mutant by: (i) in trans expression of resA; (ii) deficiency in BdbD, a thioldisulfide oxidoreductase that catalyzes formation of an intramolecular disulfide bond in apocytochrome c after transfer of the polypeptide across the cytoplasmic membrane; or (iii) by addition of the reductant dithiothreitol to the growth medium. In vivo studies of ResA showed that it is membrane-associated with its thioredoxin-like domain on the outside of the cytoplasmic membrane. Analysis of a soluble form of the protein revealed two redox reactive cysteine residues with a midpoint potential of about -340 mV at pH 7. We conclude that ResA, probably together with another thiol-disulfide oxidoreductase, CcdA, is required for the reduction of the cysteinyls in the heme binding site of apocytochrome c.},
  author       = {Erlendsson, Lydur and Acheson, Richard M. and Hederstedt, Lars and Le Brun, Nick E.},
  issn         = {1083-351X},
  language     = {eng},
  number       = {20},
  pages        = {17852--17858},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {<em>Bacillus subtilis</em> ResA is a thiol-disulfide oxidoreductase involved in cytochrome c synthesis},
  url          = {http://dx.doi.org/10.1074/jbc.M300103200},
  volume       = {278},
  year         = {2003},
}