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J Bacteriol, April 1998, p. 1869-1877, Vol. 180, No. 7
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Thioredoxin Is an Essential Protein Induced by
Multiple Stresses in Bacillus subtilis
Christian
Scharf,
Sabine
Riethdorf,
Henrik
Ernst,
Susanne
Engelmann,
Uwe
Völker,
and
Michael
Hecker*
Ernst-Moritz-Arndt-University, Institute for
Microbiology and Molecular Biology, 17487 Greifswald, Germany
Received 17 November 1997/Accepted 3 February 1998
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,
B, was required for the
initiation of transcription at the upstream site, SB, and
the promoter preceding the downstream start site, SA, was
presumably recognized by the vegetative sigma factor,
A.
In contrast to the heat-inducible,
A-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,
SA. The induction patterns of the promoters differed, with the upstream promoter displaying the typical stress induction of
B-dependent promoters. Transcription initiating at
SA, but not at SB, was also induced after
treatment with hydrogen peroxide or puromycin. Such a double control of
stress induction at two different promoters seems to be typical of a
subgroup of class III heat shock genes of B. subtilis, like
clpC, and it either allows the cells to raise the level of
the antioxidant thioredoxin after oxidative stress or allows stressed
cells to accumulate thioredoxin. These increased levels of thioredoxin
might help stressed B. subtilis cells to maintain the
native and reduced state of cellular proteins.
*
Corresponding author. Mailing address:
Ernst-Moritz-Arndt-University, Institute for Microbiology and Molecular
Biology, Friedrich-Ludwig-Jahn-Str. 15, Greifswald, 17487, Germany.
Phone: 0049-3834-864200. Fax: 0049-3834-864202. E-mail:
hecker{at}microbio7.biologie.uni-greifswald.de.

Present address: Department of Gynecological Histopathology,
University of Hamburg, Hamburg, Germany.

Present address: Laboratory for Microbiology,
Philipps-University-Marburg, Marburg, Germany.
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