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Journal of Bacteriology, June 2007, p. 4078-4086, Vol. 189, No. 11
0021-9193/07/$08.00+0 doi:10.1128/JB.01901-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.
R
,
Ben Pascoe,
Dimitris Kallifidas, and
Mark S. B. Paget*
Department of Biochemistry, School of Life Sciences, University of Sussex, Falmer, Brighton BN1 9QG, United Kingdom
Received 15 December 2006/ Accepted 23 March 2007
Streptomyces coelicolor contains paralogous versions of seven ribosomal proteins (S14, S18, L28, L31, L32, L33, and L36), which differ in their potential to bind structural zinc. The paralogues are termed C+ or C on the basis of the presence or absence of putative cysteine ligands. Here, mutational studies suggest that the C version of L31 can functionally replace its C+ paralogue only when expressed at an artificially elevated level. We show that the level of expression of four transcriptional units encoding C proteins is elevated under conditions of zinc deprivation. Zur controls the expression of three transcriptional units (including rpmG2, rpmE2, rpmB2, rpsN2, rpmF2, and possibly rpsR2). Zur also controls the expression of the znuACB operon, which is predicted to encode a high-affinity zinc transport system. Surprisingly, the zinc-responsive control of the rpmG3-rpmJ2 operon is dictated by
R, a sigma factor that was previously shown to control the response to disulfide stress in S. coelicolor. The induction of
R activity during zinc limitation establishes an important link between thiol-disulfide metabolism and zinc homeostasis.
Published ahead of print on 30 March 2007.
Supplemental material for this article may be found at http://jb.asm.org/.
These authors contributed equally to this work.
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