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Bacillus subtilis StoA is a thiol-disulfide oxidoreductase important for spore cortex synthesis

Erlendsson, Lydur LU ; Carlsson Möller, Mirja LU and Hederstedt, Lars LU (2004) In Journal of Bacteriology 186(18). p.6230-6238
Abstract
Bacillus subtilis is an endospore-forming bacterium. There are indications that protein disulfide linkages occur in spores, but the role of thiol-disulfide chemistry in spore synthesis is not understood. Thiol-disulfide oxidoreductases catalyze formation or breakage of disulfide bonds in proteins. CcdA is the only B. subtilis thiol-disulfide oxidoreductase that has previously been shown to play some role in endospore biogenesis. In this work we show that lack of the StoA (YkvV) protein results in spores sensitive to heat, lysozyme, and chloroform. Compared to CcdA deficiency, StoA deficiency results in a 100-fold-stronger negative effect on sporulation efficiency. StoA is a membrane-bound protein with a predicted thioredoxin-like domain... (More)
Bacillus subtilis is an endospore-forming bacterium. There are indications that protein disulfide linkages occur in spores, but the role of thiol-disulfide chemistry in spore synthesis is not understood. Thiol-disulfide oxidoreductases catalyze formation or breakage of disulfide bonds in proteins. CcdA is the only B. subtilis thiol-disulfide oxidoreductase that has previously been shown to play some role in endospore biogenesis. In this work we show that lack of the StoA (YkvV) protein results in spores sensitive to heat, lysozyme, and chloroform. Compared to CcdA deficiency, StoA deficiency results in a 100-fold-stronger negative effect on sporulation efficiency. StoA is a membrane-bound protein with a predicted thioredoxin-like domain probably localized in the intermembrane space of the forespore. Electron microscopy of spores of CcdA- and StoA-deficient strains showed that the spore cortex is absent in both cases. The BdbD protein catalyzes formation of disulfide bonds in proteins on the outer side of the cytoplasmic membrane but is not required for sporulation. Inactivation of bdbD was found to suppress the sporulation defect of a strain deficient in StoA. Our results indicate that StoA is a thiol-disulfide oxidoreductase that is involved in breaking disulfide bonds in cortex components or in proteins important for cortex synthesis. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Bacteriology
volume
186
issue
18
pages
6230 - 6238
publisher
American Society for Microbiology
external identifiers
  • wos:000223699900029
  • pmid:15342593
  • scopus:4444319828
ISSN
0021-9193
DOI
10.1128/JB.186.18.6230-6238.2004
language
English
LU publication?
yes
id
d643b607-5ce2-4f02-830d-5bbc539c3be1 (old id 267775)
date added to LUP
2007-10-22 15:02:25
date last changed
2017-08-10 10:07:23
@article{d643b607-5ce2-4f02-830d-5bbc539c3be1,
  abstract     = {Bacillus subtilis is an endospore-forming bacterium. There are indications that protein disulfide linkages occur in spores, but the role of thiol-disulfide chemistry in spore synthesis is not understood. Thiol-disulfide oxidoreductases catalyze formation or breakage of disulfide bonds in proteins. CcdA is the only B. subtilis thiol-disulfide oxidoreductase that has previously been shown to play some role in endospore biogenesis. In this work we show that lack of the StoA (YkvV) protein results in spores sensitive to heat, lysozyme, and chloroform. Compared to CcdA deficiency, StoA deficiency results in a 100-fold-stronger negative effect on sporulation efficiency. StoA is a membrane-bound protein with a predicted thioredoxin-like domain probably localized in the intermembrane space of the forespore. Electron microscopy of spores of CcdA- and StoA-deficient strains showed that the spore cortex is absent in both cases. The BdbD protein catalyzes formation of disulfide bonds in proteins on the outer side of the cytoplasmic membrane but is not required for sporulation. Inactivation of bdbD was found to suppress the sporulation defect of a strain deficient in StoA. Our results indicate that StoA is a thiol-disulfide oxidoreductase that is involved in breaking disulfide bonds in cortex components or in proteins important for cortex synthesis.},
  author       = {Erlendsson, Lydur and Carlsson Möller, Mirja and Hederstedt, Lars},
  issn         = {0021-9193},
  language     = {eng},
  number       = {18},
  pages        = {6230--6238},
  publisher    = {American Society for Microbiology},
  series       = {Journal of Bacteriology},
  title        = {<em>Bacillus subtilis</em> StoA is a thiol-disulfide oxidoreductase important for spore cortex synthesis},
  url          = {http://dx.doi.org/10.1128/JB.186.18.6230-6238.2004},
  volume       = {186},
  year         = {2004},
}