Affiliation:
1. Department of Environmental & Biomolecular Systems, OGI School of Science & Engineering, Oregon Health & Science University, Beaverton, Oregon
2. Department of Microbiology, HanNam University, 133 Ojung-Dong, Taeduk-Ku, Daejon 306-791, South Korea
Abstract
ABSTRACT
Spx is a global transcriptional regulator of the oxidative stress response in
Bacillus subtilis
. Its target is RNA polymerase, where it contacts the α subunit C-terminal domain. Recently, evidence was presented that Spx participates in sulfate-dependent control of organosulfur utilization operons, including the
ytmI
,
yxeI
,
ssu
, and
yrrT
operons. The
yrrT
operon includes the genes that function in cysteine synthesis from
S
-adenosylmethionine through intermediates
S
-adenosylhomocysteine, ribosylhomocysteine, homocysteine, and cystathionine. These operons are also negatively controlled by CymR, the repressor of cysteine biosynthesis operons. All of the operons are repressed in media containing cysteine or sulfate but are derepressed in medium containing the alternative sulfur source, methionine. Spx was found to negatively control the expression of these operons in sulfate medium, in part, by stimulating the expression of the
cymR
gene. In addition, microarray analysis, monitoring of
yrrT-lacZ
fusion expression, and in vitro transcription studies indicate that Spx directly activates
yrrT
operon expression during growth in medium containing methionine as sole sulfur source. These experiments have uncovered additional roles for Spx in the control of gene expression during unperturbed, steady-state growth.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
38 articles.
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