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Sensing and responding to oxidative stress through RsrA-sigmaR in Streptomyces

Reference	BBS/E/J/00004132
Principal Investigator / Supervisor	Professor Mark Buttner
Co-Investigators / Co-Supervisors
Institution	John Innes Centre
Department	John Innes Centre Department
Funding type	Research
Value (£)	44,069
Status	Completed
Type	Institute Project
Start date	01/03/1999
End date	30/04/2003
Duration	50 months

Abstract

We have identified two proteins, sigmaR and RsrA (an anti-sigma factor), that modulate expression of the thioredoxin system in response to oxidative stress in S. coelicolor. The objectives of the proposed work are (i) to identify by site-directed mutagenesis which of the 7 Cys residues are involved in the formation of the intramolecular disulphide bond that inactivates RsrA (ii) to confirm this assignment through MALDI-TOF spectroscopic analysis of tryptic peptides generated from the reduced and oxidised form of RsrA (from which the 5 other Cys residues have been removed) (iii) to confirm the in vitro biochemical data by examining the activity of the rsrA mutant alleles in vivo (iv) to identify further genes under sigmaR control (v) to determine if oxidised RsrA is a substrate for the thioredoxin system (vi) to examine the effect of up-regulating trxBA expression on the yield of the ACV-derived beta-lactam cephamycin C in S. clavuligerus.

Summary

unavailable

Committee	Closed Committee - Plant & Microbial Sciences (PMS)
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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