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Structural investigations of the release factors eRF-1 and eRF-3 and the prion-like properties of Sup35 (yeast eRF-3)

Reference	B09527
Principal Investigator / Supervisor	Dr David Barford
Co-Investigators / Co-Supervisors
Institution	Institute of Cancer Research
Department	Structural Biology
Funding type	Research
Value (£)	148,997
Status	Completed
Type	Research Grant
Start date	01/09/1998
End date	04/08/2002
Duration	47 months

Abstract

The structures of eRF-1, eRF-3 and soluble Sup35 will be determined by X-ray crystallography and the Sup35 fibres will be examined using X-ray fibre diffraction. These structures will allow insight into the mechanism of translation termination, specifically tRNA mimicry and mRNA stop codon recognition by eRF-1 and its TP- dependent regulation mediated by eRF-3. Soluble Sup35 undergoes a conformational change to form fibres in an auto-catalytic fashion that is concentration dependent and seeded by preformed fibres, similar to human prion proteins. The structures of soluble Sup35 and its fibres will provide an understanding of this process and be relevant to prion proteins that are associated with transmissible spongiform encephalopathies.

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

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