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Response regulator aspartic acid phosphatases controlling adaptation in Bacillus
Reference
C14673
Principal Investigator / Supervisor
Professor Anthony Wilkinson
Co-Investigators /
Co-Supervisors
Institution
University of York
Department
Chemistry
Funding type
Research
Value (£)
187,232
Status
Completed
Type
Research Grant
Start date
01/03/2001
End date
01/03/2004
Duration
36 months
Abstract
The hallmark of the two-component signalling systems of bacteria is their use of protein phosphorylation on histidine and aspartic acid residues. In studies of proteins controlling spore formation in Bacillus, we recently determined the first crystal structure of a protein phosphorylated on aspartic acid. Here, we plan to explore the Rap family of protein phosphatases whose substrates are protein aspartate phosphates. Many of the 11 Rap phosphatases are inhibited by cognate peptides which undergo a curious export-processing- import cycle. We propose to overproduce these enzymes and to characterise their peptide binding and phosphatase activities, with a view to determining crystal structures of the enzymes themselves and their complexes.
Summary
unavailable
Committee
Closed Committee - Biochemistry & Cell Biology (BCB)
Research Topics
X – not assigned to a current Research Topic
Research Priority
X – Research Priority information not available
Research Initiative
X - not in an Initiative
Funding Scheme
X – not Funded via a specific Funding Scheme
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