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Response to copper stress in Streptomyces lividans extends beyond genes under direct control of a copper-sensitive operon repressor protein (CsoR)

Dwarakanath, S and Chaplin, AK and Hough, MA and Rigali, S and Vijgenboom, E and Worrall, JAR (2012) 'Response to copper stress in Streptomyces lividans extends beyond genes under direct control of a copper-sensitive operon repressor protein (CsoR).' Journal of Biological Chemistry, 287 (21). 17833 - 17847. ISSN 0021-9258

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Abstract

A copper-sensitive operon repressor protein (CsoR) has been identified in Streptomyces lividans (CsoR Sl ) and found to regulate copper homeostasis with attomolar affinity for Cu(I). Solution studies reveal apo- and CuI-CsoR Sl to be a tetramer assembly, and a 1.7-Å resolution crystal structure of apo-CsoR Sl reveals that a significant conformational change is necessary to enable Cu(I) binding. In silico prediction of the CsoR regulon was confirmed in vitro (EMSA) and in vivo (RNA-seq), which highlighted that next to the csoR gene itself, the regulon consists of two Cu(I) efflux systems involving a CopZ-like copper metallochaperone protein and a CopA P 1 -type ATPase. Although deletion of csoR has only minor effects on S. lividans development when grown under high copper concentrations, mutations of the Cu(I) ligands decrease tolerance to copper as a result of the Cu(I)-CsoR mutants failing to disengage from the DNA targets, thus inhibiting the derepression of the regulon. RNA-seq experiments carried out on samples incubated with exogenous copper and a ΔcsoR strain showed that the set of genes responding to copper stress is much wider than anticipated and largely extends beyond genes targeted by CsoR. This suggests more control levels are operating and directing other regulons in copper homeostasis beside the CsoR regulon. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.

Item Type: Article
Subjects: Q Science > Q Science (General)
Q Science > QP Physiology
Divisions: Faculty of Science and Health > Biological Sciences, School of
Depositing User: Mike Hough
Date Deposited: 11 Oct 2012 21:37
Last Modified: 17 Aug 2017 18:07
URI: http://repository.essex.ac.uk/id/eprint/4044

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