Archives of Microbiology

, 192:57

The putative Bacillus subtilisl,d-transpeptidase YciB is a lipoprotein that localizes to the cell poles in a divisome-dependent manner

Original Paper

Abstract

Cell wall synthesis in bacteria is spatially organized by cytoskeletal structures. Common to all cell wall-bearing bacteria, the cytokinetic machinery localizes the cell wall synthesis to the site of septation. Recently, MinJ, a new component of the cytokinetic machinery, or divisome, of Bacillus subtilis has been described. MinJ is part of the division site selection system but also essential for correct assembly of the divisome. Here, I used the isolated PDZ domain of MinJ for co-elution experiments. One of the proteins that co-eluted was the so far uncharacterized, putative l,d-transpeptidase protein YciB. Evidence is shown that YciB localizes to the cell poles. YciB localization depends on the existence of a mature divisome, suggesting that l,d-transpeptidases are, like penicillin-binding proteins, part of the divisome.

Keywords

l,d-transpeptidase YciB Cell division Protein localization Peptidoglycan synthesis Lipoprotein 

Abbreviations

BSA

Bovine serum albumin

DAPI

4′,6-diamidino-2-phenylindole

EDTA

Ethylenediaminetetraacetic acid

FITC

Fluorescein isothiocyanate

GFP

Green fluorescent protein

IPTG

Isopropyl β-d-1-thiogalactopyranoside

LDAO

N-dodecyl-N,N-dimethylamine-N-oxide

MIC

Minimum inhibitory concentration

PAGE

Polyacrylamide gel electrophoresis

PBP

Penicillin-binding protein

PBS

Phosphate-buffered saline

PG

Peptidoglycan/murein

PMF

Peptide-mass fingerprinting

SDS

Sodium dodecyl sulfate

Copyright information

© Springer-Verlag 2009

Authors and Affiliations

  1. 1.Institute for BiochemistryUniversity of CologneCologneGermany

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