Bacillus subtilis StoA is a thiol-disulfide oxidoreductase important for spore cortex synthesis
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/267775
- author
- Erlendsson, Lydur LU ; Carlsson Möller, Mirja LU and Hederstedt, Lars LU
- organization
- publishing date
- 2004
- 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
- pmid:15342593
- 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
- 2016-04-01 12:17:49
- date last changed
- 2022-03-21 02:12:04
@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}},
doi = {{10.1128/JB.186.18.6230-6238.2004}},
volume = {{186}},
year = {{2004}},
}