BBSRC Portfolio Analyser
Award details
Characteristion of the DegP(HtrA) chaperone/ protease machine
Reference
B17814
Principal Investigator / Supervisor
Professor Dafydd Jones
Co-Investigators /
Co-Supervisors
Institution
Cardiff University
Department
School of Biosciences
Funding type
Research
Value (£)
184,544
Status
Completed
Type
Research Grant
Start date
15/02/2003
End date
15/02/2006
Duration
36 months
Abstract
Molecular chaperones and proteases monitor the folded state of other proteins. In addition to recognising non-native conformations these quality control factors distinguish substrates that can be refolded from those that need to be degraded because they are severely damaged. To investigate the molecular basis of this process, we have solved the crystal structure of DegP (HtrA), a widely conserved heat shock protein that combines refolding and proteolytic activities. A detailed structure-function analysis of DegP from E.coli is expected to provide novel insights on how a single cellular factor can channel different substrates into one of the two key pathways controlling protein stability and protein turnover.
Summary
unavailable
Committee
Closed Committee - Biomolecular Sciences (BMS)
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
I accept the
terms and conditions of use
(opens in new window)
export PDF file
back to list
new search