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The PASTA domain of penicillin-binding protein SpoVD is dispensable for endospore cortex peptidoglycan assembly in Bacillus subtilis.

In English

Författare

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.

Publiceringsår

2015

Språk

Engelska

Sidor

330-340

Publikation/Tidskrift/Serie

Microbiology

Volym

161

Issue

Online 6 January, 2014

Dokumenttyp

Artikel i tidskrift

Förlag

MAIK Nauka/Interperiodica

Ämne

  • Biological Sciences

Status

Published

ISBN/ISSN/Övrigt

  • ISSN: 1465-2080