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Role of membrane-bound thiol-disulfide oxidoreductases in endospore-forming bacteria

Carlsson Möller, Mirja LU and Hederstedt, Lars LU (2006) In Antioxidants & Redox Signaling 8(5-6). p.823-833
Abstract
Thiol-disulfide oxidoreductases catalyze formation, disruption, or isomerization of disulfide bonds between cysteine residues in proteins. Much is known about the functional roles and properties of this class of redox enzymes in vegetative bacterial cells but their involvement in sporulation has remained unknown until recently. Two membrane-embedded thiol-disulfide oxidoreductases, CcdA and StoA/SpoIVH, conditionally required for efficient production of Bacillus subtilis heat-resistant endospores, have now been identified. Properties of mutant cells lacking the two enzymes indicate new aspects in the molecular details of endospore envelope development. This mini-review presents an overview of membrane-bound thiol-disulfide oxidoreductases... (More)
Thiol-disulfide oxidoreductases catalyze formation, disruption, or isomerization of disulfide bonds between cysteine residues in proteins. Much is known about the functional roles and properties of this class of redox enzymes in vegetative bacterial cells but their involvement in sporulation has remained unknown until recently. Two membrane-embedded thiol-disulfide oxidoreductases, CcdA and StoA/SpoIVH, conditionally required for efficient production of Bacillus subtilis heat-resistant endospores, have now been identified. Properties of mutant cells lacking the two enzymes indicate new aspects in the molecular details of endospore envelope development. This mini-review presents an overview of membrane-bound thiol-disulfide oxidoreductases in the Gram-positive bacterium B. subtilis and endospore synthesis. Accumulated experimental findings on CcdA and StoA/SpoIVH are reviewed. A model for the role of these proteins in endospore cortex biogenesis in presented. (Less)
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publishing date
type
Contribution to journal
publication status
published
subject
in
Antioxidants & Redox Signaling
volume
8
issue
5-6
pages
823 - 833
publisher
Mary Ann Liebert, Inc.
external identifiers
  • wos:000238725100012
  • scopus:33745865551
ISSN
1557-7716
DOI
10.1089/ars.2006.8.823
language
English
LU publication?
yes
id
2ea8c16f-3db6-4857-bdac-f6e2cd6d43f6 (old id 404684)
date added to LUP
2016-04-01 16:41:59
date last changed
2021-08-25 04:35:36
@article{2ea8c16f-3db6-4857-bdac-f6e2cd6d43f6,
  abstract     = {Thiol-disulfide oxidoreductases catalyze formation, disruption, or isomerization of disulfide bonds between cysteine residues in proteins. Much is known about the functional roles and properties of this class of redox enzymes in vegetative bacterial cells but their involvement in sporulation has remained unknown until recently. Two membrane-embedded thiol-disulfide oxidoreductases, CcdA and StoA/SpoIVH, conditionally required for efficient production of Bacillus subtilis heat-resistant endospores, have now been identified. Properties of mutant cells lacking the two enzymes indicate new aspects in the molecular details of endospore envelope development. This mini-review presents an overview of membrane-bound thiol-disulfide oxidoreductases in the Gram-positive bacterium B. subtilis and endospore synthesis. Accumulated experimental findings on CcdA and StoA/SpoIVH are reviewed. A model for the role of these proteins in endospore cortex biogenesis in presented.},
  author       = {Carlsson Möller, Mirja and Hederstedt, Lars},
  issn         = {1557-7716},
  language     = {eng},
  number       = {5-6},
  pages        = {823--833},
  publisher    = {Mary Ann Liebert, Inc.},
  series       = {Antioxidants & Redox Signaling},
  title        = {Role of membrane-bound thiol-disulfide oxidoreductases in endospore-forming bacteria},
  url          = {http://dx.doi.org/10.1089/ars.2006.8.823},
  doi          = {10.1089/ars.2006.8.823},
  volume       = {8},
  year         = {2006},
}