Phosphoproteomic analysis of Escherichia coli
EMSL Project ID
48210
Abstract
Ser/Thr phosphorylation is a key mechanism of cellular regulation in eukaryotes, but its role in prokaryotes is far less clear. In the past ~5 years, phosphoproteomic approaches have found that a large number of proteins (>75) in bacterial cells are phosphorylated on either a Ser or a Thr residue. Although the particular kinase(s) responsible for these modifications are mostly not known, Ser/Thr kinases have been described in phylogenetically diverse bacteria. They mediate extracellular processes including biofilm formation and the production of the bacterial cell wall. A key goal of microbiology is the identification of the substrates of these kinases in order to understand the regulation of these processes. Our proposed work will identify the substrates of a single Ser/Thr kinase in the bacterium Escherichia coli, and thereby offer new insight into the strategies used by this important organism to regulate the production of secreted, extracellular proteins. E. coli is one of the most favored industrial microorganisms and is an important organism for the production of cellulose degrading enzymes [1]. The automated IMAC technology developed by Dr. Paša-Toli? at EMSL will provide an essential and novel basis for our analysis. Thus, this work is central to the mission of the EMSL to provide solutions to the nation's energy production challenges such as those provided by biofuel production.
Project Details
Project type
Limited Scope
Start Date
2013-12-02
End Date
2014-02-01
Status
Closed
Released Data Link
Team
Principal Investigator