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The structural basis of assembly of the tim9/10 translocase in the mitochondrial intermembrane space
Reference
B12957
Principal Investigator / Supervisor
Professor Kostas Tokatlidis
Co-Investigators /
Co-Supervisors
Institution
The University of Manchester
Department
Life Sciences
Funding type
Research
Value (£)
110,950
Status
Completed
Type
Research Grant
Start date
01/08/2000
End date
01/08/2002
Duration
24 months
Abstract
Polytopic proteins of the mitochondrial inner membrane fulfil crucial cellular functions and are imported into mitochondria by a specialised translocation system. This is a complex of soluble, zinc-binding proteins (Tim9, 10 and 12) that transiently binds the hydrophobic carriers facilitating thus their passage across the aqueous intermembrane space. The subunits of this novel chaperone system are themselves imported from the cytosol into the intermembrane space where they assemble in heterooligomeric complexes. The aim of this project is to investigate the structural basis of this macromolecular assembly by studying the sequence motifs involved in import and assembly of the Tim proteins and the underlying protein-protein interactions.
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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