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J Bacteriol, June 1998, p. 2895-2900, Vol. 180, No. 11
Institut für Genetik,
Received 23 December 1997/Accepted 24 March 1998
The chaperone-encoding groESL and dnaK
operons constitute the CIRCE regulon of Bacillus subtilis.
Both operons are under negative control of the repressor protein HrcA,
which interacts with the CIRCE operator and whose activity is modulated
by the GroESL chaperone machine. In this report, we demonstrate that
induction of the CIRCE regulon can also be accomplished by ethanol
stress and puromycin. Introduction of the hrcA gene and a
transcriptional fusion under the control of the CIRCE operator into
Escherichia coli allowed induction of this fusion by heat
shock, ethanol stress, and overproduction of GroESL substrates. The
expression level of this hrcA-bgaB fusion inversely
correlated with the amount of GroE machinery present in the cells.
Therefore, all inducing conditions seem to lead to induction via
titration of the GroE chaperonins by the increased level of nonnative
proteins formed. Puromycin treatment failed to induce the
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Nonnative Proteins Induce Expression of the Bacillus
subtilis CIRCE Regulon
B-dependent general stress regulon, indicating that
nonnative proteins in general do not trigger this response.
Reconstitution of HrcA-dependent heat shock regulation of B. subtilis in E. coli and complementation of E. coli groESL mutants by B. subtilis groESL indicate
that the GroE chaperonin systems of the two bacterial species are
functionally exchangeable.
*
Corresponding author. Mailing address:
Philipps-Universität, Laboratorium für Mikrobiologie,
Karl-von-Frisch-Strasse, 35043 Marburg, Germany. Phone: 49 6421 283478. Fax: 49 6421 288979. E-mail:
voelker{at}su1701.biologie.uni-marburg.de.
J Bacteriol, June 1998, p. 2895-2900, Vol. 180, No. 11
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
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