Evidence from artificial septal targeting and site-directed mutagenesis that residues in the extracytoplasmic beta domain of DivIB mediate its interaction with the divisomal transpeptidase PBP 2B

Rowland, Susan L., Wadsworth, Kimberly D., Robson, Scott A., Robichon, Carine, Beckwith, Jon and King, Glenn F. (2010) Evidence from artificial septal targeting and site-directed mutagenesis that residues in the extracytoplasmic beta domain of DivIB mediate its interaction with the divisomal transpeptidase PBP 2B. Journal of Bacteriology, 192 23: 6116-6125. doi:10.1128/JB.00783-10

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Author Rowland, Susan L.
Wadsworth, Kimberly D.
Robson, Scott A.
Robichon, Carine
Beckwith, Jon
King, Glenn F.
Title Evidence from artificial septal targeting and site-directed mutagenesis that residues in the extracytoplasmic beta domain of DivIB mediate its interaction with the divisomal transpeptidase PBP 2B
Formatted title
Evidence from artificial septal targeting and site-directed mutagenesis that residues in the extracytoplasmic β domain of DivIB mediate its interaction with the divisomal transpeptidase PBP 2B
Journal name Journal of Bacteriology   Check publisher's open access policy
ISSN 0021-9193
1067-8832
1098-5530
Publication date 2010-12
Sub-type Article (original research)
DOI 10.1128/JB.00783-10
Open Access Status File (Publisher version)
Volume 192
Issue 23
Start page 6116
End page 6125
Total pages 10
Place of publication Washington, DC, United States
Publisher American Society for Microbiology
Collection year 2011
Language eng
Formatted abstract
Bacterial cytokinesis is achieved through the coordinated action of a multiprotein complex known as the divisome. The Escherichia coli divisome is comprised of at least 10 essential proteins whose individual functions are mostly unknown. Most divisomal proteins have multiple binding partners, making it difficult to pinpoint epitopes that mediate pairwise interactions between these proteins. We recently introduced an artificial septal targeting approach that allows the interaction between pairs of proteins to be studied in vivo without the complications introduced by other interacting proteins (C. Robichon, G. F. King, N. W. Goehring, and J. Beckwith, J. Bacteriol. 190:6048-6059, 2008). We have used this approach to perform a molecular dissection of the interaction between Bacillus subtilis DivIB and the divisomal transpeptidase PBP 2B, and we demonstrate that this interaction is mediated exclusively through the extracytoplasmic domains of these proteins. Artificial septal targeting in combination with mutagenesis experiments revealed that the C-terminal region of the β domain of DivIB is critical for its interaction with PBP 2B. These findings are consistent with previously defined loss-of-function point mutations in DivIB as well as the recent demonstration that the β domain of DivIB mediates its interaction with the FtsL-DivIC heterodimer. These new results have allowed us to construct a model of the DivIB/PBP 2B/FtsL/DivIC quaternary complex that strongly implicates DivIB, FtsL, and DivIC in modulating the transpeptidase activity of PBP 2B. 
Keyword Cell division proteins
Bacillus-subtilis
Escherichia-coli
Streptococcus-pneumoniae
Assembly dynamics
Clinical isolate
Mutant alleles
FTSI PBP3
Localization
Ring
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: Official 2011 Collection
 
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Created: Sun, 05 Dec 2010, 00:09:49 EST