Penicillin-binding protein SpoVD disulfide is a target for StoA in Bacillus subtilis forespores.
(2010) In Molecular Microbiology 75(1). p.46-60- Abstract
- Summary The bacterial endospore is a dormant and heat-resistant form of life. StoA (SpoIVH) in Bacillus subtilis is a membrane-bound thioredoxin-like protein involved in endospore cortex synthesis. It is proposed to reduce disulfide bonds in hitherto unknown proteins in the inter-membrane compartment of developing forespores. Starting with a bioinformatic analysis combined with mutant studies we identified the sporulation-specific, high molecular weight, class B penicillin-binding protein SpoVD as a putative target for StoA. We then demonstrate that SpoVD is a membrane-bound protein with two exposed redox-active cysteine residues. Structural modelling of SpoVD, based on the well characterized orthologue PBP2x of Streptococcus pneumoniae,... (More)
- Summary The bacterial endospore is a dormant and heat-resistant form of life. StoA (SpoIVH) in Bacillus subtilis is a membrane-bound thioredoxin-like protein involved in endospore cortex synthesis. It is proposed to reduce disulfide bonds in hitherto unknown proteins in the inter-membrane compartment of developing forespores. Starting with a bioinformatic analysis combined with mutant studies we identified the sporulation-specific, high molecular weight, class B penicillin-binding protein SpoVD as a putative target for StoA. We then demonstrate that SpoVD is a membrane-bound protein with two exposed redox-active cysteine residues. Structural modelling of SpoVD, based on the well characterized orthologue PBP2x of Streptococcus pneumoniae, confirmed that a disulfide bond can form close to the active site of the penicillin-binding domain restricting access of enzyme substrate or functional association with other cortex biogenic proteins. Finally, by exploiting combinations of mutations in the spoVD, stoA and ccdA genes in B. subtilis cells, we present strong in vivo evidence that supports the conclusion that StoA functions to specifically break the disulfide bond in the SpoVD protein in the forespore envelope. The findings contribute to our understanding of endospore biogenesis and open a new angle to regulation of cell wall synthesis and penicillin-binding protein activity. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1511875
- author
- Liu, Yiming LU ; Carlsson Möller, Mirja LU ; Petersen, Lise ; Söderberg, Christopher LU and Hederstedt, Lars LU
- organization
- publishing date
- 2010
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Molecular Microbiology
- volume
- 75
- issue
- 1
- pages
- 46 - 60
- publisher
- Wiley-Blackwell
- external identifiers
-
- wos:000273068500006
- scopus:72949112015
- pmid:19919673
- ISSN
- 1365-2958
- DOI
- 10.1111/j.1365-2958.2009.06964.x
- language
- English
- LU publication?
- yes
- id
- f3c7c6b2-9414-40e5-9672-5e4fcc66bee7 (old id 1511875)
- date added to LUP
- 2016-04-01 10:18:49
- date last changed
- 2022-01-25 22:01:48
@article{f3c7c6b2-9414-40e5-9672-5e4fcc66bee7,
abstract = {{Summary The bacterial endospore is a dormant and heat-resistant form of life. StoA (SpoIVH) in Bacillus subtilis is a membrane-bound thioredoxin-like protein involved in endospore cortex synthesis. It is proposed to reduce disulfide bonds in hitherto unknown proteins in the inter-membrane compartment of developing forespores. Starting with a bioinformatic analysis combined with mutant studies we identified the sporulation-specific, high molecular weight, class B penicillin-binding protein SpoVD as a putative target for StoA. We then demonstrate that SpoVD is a membrane-bound protein with two exposed redox-active cysteine residues. Structural modelling of SpoVD, based on the well characterized orthologue PBP2x of Streptococcus pneumoniae, confirmed that a disulfide bond can form close to the active site of the penicillin-binding domain restricting access of enzyme substrate or functional association with other cortex biogenic proteins. Finally, by exploiting combinations of mutations in the spoVD, stoA and ccdA genes in B. subtilis cells, we present strong in vivo evidence that supports the conclusion that StoA functions to specifically break the disulfide bond in the SpoVD protein in the forespore envelope. The findings contribute to our understanding of endospore biogenesis and open a new angle to regulation of cell wall synthesis and penicillin-binding protein activity.}},
author = {{Liu, Yiming and Carlsson Möller, Mirja and Petersen, Lise and Söderberg, Christopher and Hederstedt, Lars}},
issn = {{1365-2958}},
language = {{eng}},
number = {{1}},
pages = {{46--60}},
publisher = {{Wiley-Blackwell}},
series = {{Molecular Microbiology}},
title = {{Penicillin-binding protein SpoVD disulfide is a target for StoA in <em>Bacillus subtilis</em> forespores.}},
url = {{http://dx.doi.org/10.1111/j.1365-2958.2009.06964.x}},
doi = {{10.1111/j.1365-2958.2009.06964.x}},
volume = {{75}},
year = {{2010}},
}