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Forespore targeting of SpoVD in Bacillus subtilis is mediated by the N-terminal part of the protein.

Sidarta, Margareth LU ; Hederstedt, Lars LU and Bukowska-Faniband, Ewa LU (2018) In Journal of Bacteriology 200(e00163-18).
Abstract
SpoVD and PBP4b are structurally very similar high-molecular-weight, class B penicillin-binding proteins produced early during sporulation in Bacillus subtilis. SpoVD is known to be essential for endospore cortex synthesis and thereby the production of heat-resistant spores. The role of PBP4b is still enigmatic. Both proteins are synthesized in the cytoplasm of the mother cell. PBP4b remains in the cytoplasmic membrane of the mother cell, whereas SpoVD accumulates in the forespore outer membrane. By the use of SpoVD/PBP4b chimeras with swapped protein domains, we show that the N-terminal part of SpoVD, containing the single transmembrane region, determines the forespore targeting of the protein.
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Bacillus subtilis, endospores, penicillin-binding proteins, protein structure-function, protein targeting, sporulation
in
Journal of Bacteriology
volume
200
issue
e00163-18
pages
14 pages
publisher
American Society for Microbiology
external identifiers
  • scopus:85048301288
ISSN
0021-9193
DOI
10.1128/JB.00163-18
language
English
LU publication?
yes
id
58d063db-9bc3-456e-9fd1-66297ab176c7
date added to LUP
2018-06-20 09:46:12
date last changed
2019-10-29 05:28:07
@article{58d063db-9bc3-456e-9fd1-66297ab176c7,
  abstract     = {SpoVD and PBP4b are structurally very similar high-molecular-weight, class B penicillin-binding proteins produced early during sporulation in Bacillus subtilis. SpoVD is known to be essential for endospore cortex synthesis and thereby the production of heat-resistant spores. The role of PBP4b is still enigmatic. Both proteins are synthesized in the cytoplasm of the mother cell. PBP4b remains in the cytoplasmic membrane of the mother cell, whereas SpoVD accumulates in the forespore outer membrane. By the use of SpoVD/PBP4b chimeras with swapped protein domains, we show that the N-terminal part of SpoVD, containing the single transmembrane region, determines the forespore targeting of the protein. },
  author       = {Sidarta, Margareth and Hederstedt, Lars and Bukowska-Faniband, Ewa},
  issn         = {0021-9193},
  keyword      = {Bacillus subtilis,endospores,penicillin-binding proteins,protein structure-function,protein targeting,sporulation},
  language     = {eng},
  number       = {e00163-18},
  pages        = {14},
  publisher    = {American Society for Microbiology},
  series       = {Journal of Bacteriology},
  title        = {Forespore targeting of SpoVD in Bacillus subtilis is mediated by the N-terminal part of the protein.},
  url          = {http://dx.doi.org/10.1128/JB.00163-18},
  volume       = {200},
  year         = {2018},
}