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Response regulator aspartic acid phosphatases controlling adaptation in Bacillus

ReferenceC14673
Principal Investigator / Supervisor Professor Anthony Wilkinson
Co-Investigators /
Co-Supervisors
Institution University of York
DepartmentChemistry
Funding typeResearch
Value (£) 187,232
StatusCompleted
TypeResearch Grant
Start date 01/03/2001
End date 01/03/2004
Duration36 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 TopicsX – not assigned to a current Research Topic
Research PriorityX – Research Priority information not available
Research Initiative X - not in an Initiative
Funding SchemeX – not Funded via a specific Funding Scheme
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