The PASTA domain of penicillin-binding protein SpoVD is dispensable for endospore cortex peptidoglycan assembly in Bacillus subtilis.
Author
Summary, in English
Peptidoglycan is the major structural component of the bacterial cell wall. Penicillin-binding proteins (PBPs), located at the exterior of the cytoplasmic membrane, play a major role in peptidoglycan synthesis and remodelling. A PASTA domain (penicillin-binding protein and serine/threonine kinase associated domain) of about 65 residues is found at the C-terminal end of some PBPs and eukaryotic-like protein serine/threonine kinases in a variety of bacteria. The function of PASTA domains is not understood but some of them are thought to bind uncrosslinked peptidoglycan. Bacillus subtilis has sixteen different PBPs but only two of them, Pbp2b and SpoVD, contain a PASTA domain. SpoVD is specific for sporulation and essential for endospore cortex peptidoglycan synthesis. We have studied the role of the PASTA domain in SpoVD by deleting this domain and analyzed effects on endospore formation and subcellular localization of SpoVD. Our results demonstrate that the PASTA domain in SpoVD is not essential for cortex synthesis and not important for targeting SpoVD to the forespore outer membrane during sporulation.
Department/s
Publishing year
2015
Language
English
Pages
330-340
Publication/Series
Microbiology
Volume
161
Issue
Online 6 January, 2014
Document type
Journal article
Publisher
MAIK Nauka/Interperiodica
Topic
- Biological Sciences
Status
Published
ISBN/ISSN/Other
- ISSN: 1465-2080