Award details

Structure and biogenesis-function relationships in three domains of DipZ a novel transmembrane disulphide reductase

Reference	C11888
Principal Investigator / Supervisor	Professor Stuart John Ferguson
Co-Investigators / Co-Supervisors
Institution	University of Oxford
Department	Biochemistry
Funding type	Research
Value (£)	182,028
Status	Completed
Type	Research Grant
Start date	01/05/2000
End date	01/02/2004
Duration	45 months

Abstract

DipZ is a novel transmembrane disulphide reductase, widely distributed amongst prokaryotes, but also with an orthologue in chloroplasts, that participates in the post- translational formation of disulphide bonds and c-type cytochromes in the bacterial periplasm; it is also involved in conferring resistance to heavy metals. We have recently established that E. coli DipZ has three functional domains, each bearing a pair of highly conserved cysteines that are differentially required for its functions. This project aims to elucidate the roles of these domains, including the intriguing eight helix transmembrane domain with its putative disulphide bond, in the various functions of DipZ. A variety of experimental approaches will be used.

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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