PMID: 9537387Apr 16, 1998Paper

Thioredoxin is an essential protein induced by multiple stresses in Bacillus subtilis

Journal of Bacteriology
C ScharfMichael Hecker

Abstract

Thioredoxin, a small, ubiquitous protein which participates in redox reactions through the reversible oxidation of its active center dithiol to a disulfide, is an essential protein in Bacillus subtilis. A variety of stresses, including heat or salt stress or ethanol treatment, strongly enhanced the synthesis of thioredoxin in B. subtilis. The stress induction of the monocistronic trxA gene encoding thioredoxin occurs at two promoters. The general stress sigma factor, sigmaB, was required for the initiation of transcription at the upstream site, S(B), and the promoter preceding the downstream start site, S(A), was presumably recognized by the vegetative sigma factor, sigmaA. In contrast to the heat-inducible, sigmaA-dependent promoters preceding the chaperone-encoding operons groESL and dnaK, no CIRCE (for controlling inverted repeat of chaperone expression) was present in the vicinity of the start site, S(A). The induction patterns of the promoters differed, with the upstream promoter displaying the typical stress induction of sigmaB-dependent promoters. Transcription initiating at S(A), but not at S(B), was also induced after treatment with hydrogen peroxide or puromycin. Such a double control of stress induction at two differ...Continue Reading

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Citations

Feb 13, 1999·Molecular Microbiology·F Narberhaus
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