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Transpeptidase activity of penicillin-binding protein SpoVD in peptidoglycan synthesis conditionally depends on the disulfide reductase StoA

Hederstedt, Lars LU and Bukowska-Faniband, Ewa LU (2017) In Molecular Microbiology 105. p.98-114
Abstract
Endospore cortex peptidoglycan synthesis is not
required for bacterial growth but essential for endo-
spore heat resistance. It therefore constitutes an
amenable system for research on peptidoglycan bio-
genesis. The Bacillus subtilis sporulation-specific
class B penicillin-binding protein (PBP) SpoVD and
many homologous PBPs contain two conserved cys-
teine residues of unknown function in the transpepti-
dase domain – one as residue x in the SxN catalytic
site motif and the other in a flexible loop near the cat-
alytic site. A disulfide bond between these residues
blocks the function of SpoVD in cortex synthesis.
With a combination of experiments with purified pro-
teins and B. subtilis... (More)
Endospore cortex peptidoglycan synthesis is not
required for bacterial growth but essential for endo-
spore heat resistance. It therefore constitutes an
amenable system for research on peptidoglycan bio-
genesis. The Bacillus subtilis sporulation-specific
class B penicillin-binding protein (PBP) SpoVD and
many homologous PBPs contain two conserved cys-
teine residues of unknown function in the transpepti-
dase domain – one as residue x in the SxN catalytic
site motif and the other in a flexible loop near the cat-
alytic site. A disulfide bond between these residues
blocks the function of SpoVD in cortex synthesis.
With a combination of experiments with purified pro-
teins and B. subtilis mutant cells, it was shown that
in active SpoVD the two cysteine residues most prob-
ably interact by hydrogen bonding and that this is
important for peptidoglycan synthesis in vivo. It was
furthermore demonstrated that the sporulation-
specific thiol-disulfide oxidoreductase StoA reduces
SpoVD and that requirement of StoA for cortex syn-
thesis can be suppressed by two completely different
types of structural alterations in SpoVD. It is con-
cluded that StoA plays a critical role mainly during
maturation of SpoVD in the forespore outer mem-
brane. The findings advance our understanding of
essential PBPs and redox control of extra-
cytoplasmic protein disulfides in bacterial cells. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Molecular Microbiology
volume
105
pages
98 - 114
publisher
Wiley-Blackwell
external identifiers
  • scopus:85018274701
  • wos:000403906500006
ISSN
1365-2958
DOI
10.1111/mmi.13689
language
English
LU publication?
yes
id
a4b2aca9-8c51-41cc-96ab-f42a69399eb7
date added to LUP
2017-07-17 11:36:52
date last changed
2017-09-18 11:38:27
@article{a4b2aca9-8c51-41cc-96ab-f42a69399eb7,
  abstract     = {Endospore cortex peptidoglycan synthesis is not<br/>required for bacterial growth but essential for endo-<br/>spore heat resistance. It therefore constitutes an<br/>amenable system for research on peptidoglycan bio-<br/>genesis. The Bacillus subtilis sporulation-specific<br/>class B penicillin-binding protein (PBP) SpoVD and<br/>many homologous PBPs contain two conserved cys-<br/>teine residues of unknown function in the transpepti-<br/>dase domain – one as residue x in the SxN catalytic<br/>site motif and the other in a flexible loop near the cat-<br/>alytic site. A disulfide bond between these residues<br/>blocks the function of SpoVD in cortex synthesis.<br/>With a combination of experiments with purified pro-<br/>teins and B. subtilis mutant cells, it was shown that<br/>in active SpoVD the two cysteine residues most prob-<br/>ably interact by hydrogen bonding and that this is<br/>important for peptidoglycan synthesis in vivo. It was<br/>furthermore demonstrated that the sporulation-<br/>specific thiol-disulfide oxidoreductase StoA reduces<br/>SpoVD and that requirement of StoA for cortex syn-<br/>thesis can be suppressed by two completely different<br/>types of structural alterations in SpoVD. It is con-<br/>cluded that StoA plays a critical role mainly during<br/>maturation of SpoVD in the forespore outer mem-<br/>brane. The findings advance our understanding of<br/>essential PBPs and redox control of extra-<br/>cytoplasmic protein disulfides in bacterial cells.},
  author       = {Hederstedt, Lars and Bukowska-Faniband, Ewa},
  issn         = {1365-2958},
  language     = {eng},
  pages        = {98--114},
  publisher    = {Wiley-Blackwell},
  series       = {Molecular Microbiology},
  title        = {Transpeptidase activity of penicillin-binding protein SpoVD in peptidoglycan synthesis conditionally depends on the disulfide reductase StoA},
  url          = {http://dx.doi.org/10.1111/mmi.13689},
  volume       = {105},
  year         = {2017},
}