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Characterisation of the proteases involved in the processing of the small ubiquitin-like modifier protein (SUMO-1)

Reference	C12098
Principal Investigator / Supervisor	Dr Graham Kemp
Co-Investigators / Co-Supervisors	Professor Ronald Hay
Institution	University of St Andrews
Department	Biology
Funding type	Research
Value (£)	216,892
Status	Completed
Type	Research Grant
Start date	25/10/1999
End date	25/07/2003
Duration	45 months

Abstract

Tagging of proteins with SUMO-1 influences subcellular location, susceptibility to ubiquitin- mediated degradation and is required for cell-cycle progression. This project aims to isolate and characterise two proteolytic activities involved in the regulation of SUMO-1 activity. One activity removes 4 amino acids from the C-terminus of SUMO-1 to expose the glycine to which conjugation occurs. In vivo virtually all SUMO-1 is present in protein conjugates and the other proteolytic activity recycles SUMO-1 by cleavage of the isopeptide bond. These proteases will be purified and cDNA copies of the genes isolated. Recombinant proteases will be utilised to analyse substrate recognition and determine enzyme mechanisms. The fate of these proteins in response to cell cycle and extracellular signals will be determined with specific antibodies, and their role in vivo will be examined by transfection experiments.

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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