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A molecular dissection of the prion-forming domain of the yeast Sup35p prion protein
Reference
G13284
Principal Investigator / Supervisor
Professor Emeritus Mick Tuite
Co-Investigators /
Co-Supervisors
Institution
University of Kent
Department
Sch of Biosciences
Funding type
Research
Value (£)
164,036
Status
Completed
Type
Research Grant
Start date
17/07/2000
End date
17/07/2003
Duration
36 months
Abstract
The yeast Sup35p protein can be converted into a high molecular weight aggregate via a mechanism analogous to mammalian prion conversion. The amino terminal 123 amino acids (the prion- forming domain: NPD) of Sup35p are essential for this conversion. This project will undertake an in vitro and in vivo analysis of the Sup35p NPD focusing in particular on the number and amino acid composition of the five oligopeptide repeats in the NPD. The role of the central M region in prion conversion will also be examined. Studies with the Candida albicans Sup35p NPD will be used to explore the importance of the NPD in providing a species barrier to yeast prion conversion.
Summary
unavailable
Committee
Closed Committee - Genes & Developmental Biology (GDB)
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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