Award details

Proof-reading of folded proteins by the Escherichia coli Tat machinery

Reference	BBS/E/J/0000A215
Principal Investigator / Supervisor	Professor Tracy Palmer
Co-Investigators / Co-Supervisors
Institution	John Innes Centre
Department	John Innes Centre Department
Funding type	Research
Value (£)	119,222
Status	Completed
Type	Institute Project
Start date	01/12/2004
End date	30/11/2007
Duration	36 months

Abstract

The Tat protein transport system has the remarkable ability of being able to move folded substrate proteins across the ionically tight bacterial cytoplasmic membrane. We have identified a number of mutations in the TatB component of the Tat machinery that bypasses the proof-reading capacity of the Tat system, thus allowing the transport of both folded and unfolded substrates. We aim to assess how the proof-reading function of the Tat translocase is achieved. We will use a genetic approach to identify further mutations in TatB and in other Tat components that allow export of unfolded substrate proteins. We will focus on mutations in TatB to understand how proof-reading is achieved. Using an in vitro transport assay system we will ascertain whether this is a property of the TatB protein itself, or whether it is mediated by soluble cytoplasmic factors. Finally we will assess whether TatB acts in concert with the TatC protein to carry out its proof-reading function.

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

I accept the terms and conditions of use (opens in new window)

export PDF file

back to list new search