JB Accepts, published online ahead of print on 11 July 2008

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J. Bacteriol. doi:10.1128/JB.00763-08
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Salmonella enterica sv. Typhimurium BipA Exhibits Two Distinct Ribosome Binding Modes

Megan A. deLivron and Victoria L. Robinson^*

Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269

^* To whom correspondence should be addressed. Email: victoria.robinson{at}uconn.edu.

BipA is a highly conserved prokaryotic GTPase that functions to influence numerous cellular processes in bacteria. In Escherichia coli and Salmonella typhimurium, BipA has been implicated in controlling bacterial motility, modulating attachment and effacement (A/E) processes, upregulating the expression of virulence genes and is also responsible for avoidance of host defense mechanisms. In addition, BipA is thought to be involved in bacterial stress responses such as those associated with virulence, temperature and symbiosis. Thus, BipA is necessary for securing bacterial survival and successful invasion of the host. Steady state kinetic analysis and pelleting assays were used to assess the GTPase and ribosome binding properties of S. enterica BipA. Under normal bacterial growth, BipA associates with the ribosome in the GTP-bound state. However, using sucrose density gradients, we demonstrate that the association of BipA and the ribosome is altered during stress conditions in bacteria similar to those experienced during virulence. Data are presented to show that this differential binding is brought about by the presence of ppGpp, an alarmone that signals the onset of stress-related events in bacteria.

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