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J Bacteriol, July 1998, p. 3715-3718, Vol. 180, No. 14
Department of Microbiology, New York
University School of Medicine, New York, NY 10016
Received 24 February 1998/Accepted 11 May 1998
Protein and mRNA levels of heat-labile enterotoxin (LT) of
Escherichia coli are highest at 37°C, and they
decrease gradually as temperature is decreased. This temperature
effect is eliminated in an Hns
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Temperature Regulation of Heat-Labile Enterotoxin (LT) Synthesis
in Escherichia coli Is Mediated by an Interaction
of H-NS Protein with the LT A-Subunit DNA
and
mutant.
Deletion of portions of DNA coding for the LT A subunit also
results in an increase in LT expression at low temperatures, suggesting
that the H-NS protein causes inhibition of transcription at low
temperatures by interacting with the LT A-subunit DNA. The region
that interacts with H-NS is referred to as the downstream regulatory
element (DRE). Plasmids in an hns strain from which the DRE
has been deleted still produce elevated levels of LT at 18°C, suggesting that intact DRE is not required for transcription from the LT promoter.
*
Corresponding author. Mailing address: Department of
Microbiology, New York University School of Medicine, 550 First Ave., New York, NY 10016. Phone: (212) 263-5322. Fax: (212) 263-8276. E-mail:
maasw01{at}mcrcr6.med.nyu.edu.
Present address: Department of Biology, Long Island
University-Brooklyn Campus, Brooklyn, NY 11201.
J Bacteriol, July 1998, p. 3715-3718, Vol. 180, No. 14
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
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