The divisomal protein DivIB contains multiple epitopes that mediate its recruitment to incipient division sites

Wadswoth, Kimberly D., Rowland, Susan L., Harry, Elizabeth J. and King, Glenn F. (2008) The divisomal protein DivIB contains multiple epitopes that mediate its recruitment to incipient division sites. Molecular Microbiology, 67 5: 1143-1155. doi:10.1111/j.1365-2958.2008.06114.x


Author Wadswoth, Kimberly D.
Rowland, Susan L.
Harry, Elizabeth J.
King, Glenn F.
Title The divisomal protein DivIB contains multiple epitopes that mediate its recruitment to incipient division sites
Journal name Molecular Microbiology   Check publisher's open access policy
ISSN 0950-382X
1365-2958
Publication date 2008-03-01
Year available 2008
Sub-type Article (original research)
DOI 10.1111/j.1365-2958.2008.06114.x
Open Access Status Not yet assessed
Volume 67
Issue 5
Start page 1143
End page 1155
Total pages 13
Place of publication Oxford, U.K.
Publisher Wiley-Blackwell Publishing
Language eng
Subject 320401 Medical Bacteriology
730100 Clinical (Organs, Diseases and Abnormal Conditions)
C1
060501 Bacteriology
Abstract Bacterial cytokinesis is orchestrated by an assembly of essential cell division proteins that form a supramolecular structure known as the divisome. DivIB and its orthologue FtsQ are essential members of the divisome in Gram-positive and Gram-negative bacteria respectively. DivIB is a bitopic membrane protein composed of an N-terminal cytoplasmic domain, a single-pass transmembrane domain, and a C-terminal extracytoplasmic region comprised of three separate protein domains. A molecular dissection approach was used to determine which of these domains are essential for recruitment of DivIB to incipient division sites and for its cell division functions. We show that DivIB has three molecular epitopes that mediate its localization to division septa; two epitopes are encoded within the extracytoplasmic region while the third is located in the transmembrane domain. It is proposed that these epitopes represent sites of interaction with other divisomal proteins, and we have used this information to develop a model of the way in which DivIB and FtsQ are integrated into the divisome. Remarkably, two of the three DivIB localization epitopes are dispensable for vegetative cell division; this suggests that the divisome is assembled using a complex network of protein–protein interactions, many of which are redundant and likely to be individually non-essential. © 2008 The Authors Journal compilation © 2008 Blackwell Publishing Ltd.
Keyword Bacterial cell division
Bacillus-subtilis
Escherichia-coli
Streptococcus-pneumoniae
Septal localization
Molecular dissection approach
Divisomal proteins
DivIB
Bacterial cytokinesis
Q-Index Code C1
Q-Index Status Confirmed Code
Grant ID AI48583
Institutional Status UQ

 
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