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Molecular mechanisms in the binding hydrolysis and exchange of GTP in the initiation of eukaryotic mRNA translation
Reference
C04765
Principal Investigator / Supervisor
Professor Christopher Proud
Co-Investigators /
Co-Supervisors
Institution
University of Dundee
Department
College of Life Sciences
Funding type
Research
Value (£)
150,575
Status
Completed
Type
Research Grant
Start date
29/01/1996
End date
29/06/1999
Duration
41 months
Abstract
This proposal addresses the molecular mechanisms involved in initiation of eukaryotic mRNA translation, especially the initiation factors (eIF's) involved in binding and hydrolysing GTP, and in exchanging GDP for GTP. GTP is bound by eIF-2 and later hydrolysed to GDP. It is not clear whether GTP is hydrolysed by eIF-2 itself, or by eIF-5. We will study this using pure eIF-2 and eIF-5, and will use site-directed mutagenesis to study the roles of specific residues in eIF-2 (gamma-subunit) and eIF-5. Regenerating active [eIF-2.GTP] requires eIF- 2B. Its catalytic mechanism is controversial and we will clarify this using various approaches including radiotracer and fluorescence assays of GDP/GTP exchange and protein chemical analysis of formation of [eIF-2/2B] complexes. eIF-2B activity is a key control point : we will study interplay between different allosteric effectors of eIF-2B and their relationship to the phosphorylation of eIF-2B.
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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