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

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 dna

SUBMITTER: Scharf C 

PROVIDER: S-EPMC107102 | biostudies-literature | 1998 Apr

REPOSITORIES: biostudies-literature