Bacillus subtilis ResA is a thiol-disulfide oxidoreductase involved in cytochrome c synthesis
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/310877
- author
- Erlendsson, Lydur LU ; Acheson, Richard M. ; Hederstedt, Lars LU and Le Brun, Nick E.
- organization
- publishing date
- 2003
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 278
- issue
- 20
- pages
- 17852 - 17858
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- wos:000182838300034
- scopus:0038381449
- pmid:12637552
- 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
- 2016-04-01 11:56:34
- date last changed
- 2022-03-28 17:55:48
@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 = {{American Society for Biochemistry and Molecular Biology}},
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}},
doi = {{10.1074/jbc.M300103200}},
volume = {{278}},
year = {{2003}},
}