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.

Journal of Bacteriology
Julie D Trachman, W K Maas

Abstract

Protein and mRNA levels of heat-labile enterotoxin (LT) of Escherichia coli are highest at 37 degrees C, and they decrease gradually as temperature is decreased. This temperature effect is eliminated in an Hns- 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 degrees C, suggesting that intact DRE is not required for transcription from the LT promoter.

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Citations

Dec 17, 2008·Infection and Immunity·Maria D Bodero, George P Munson
May 4, 2016·Environmental Science and Pollution Research International·Akebe Luther King AbiaMaggy Ndombo Benteke Momba
Feb 6, 2020·Brazilian Journal of Microbiology : [publication of the Brazilian Society for Microbiology]·Juliana Falcão RodriguesLuís Carlos de Souza Ferreira
Sep 13, 2006·FEMS Immunology and Medical Microbiology·Melissa Ang Simões LasaroLuís Carlos de Souza Ferreira
Sep 12, 2002·Biological Chemistry·Oliver Schröder, Rolf Wagner
Jun 1, 2010·Toxins·Benjamin Mudrak, Meta J Kuehn
Oct 17, 2001·Journal of Molecular Biology·N Delihas, S Forst
Jan 1, 2006·EcoSal Plus·Michael G Jobling, Randall K Holmes
Jan 1, 2006·EcoSal Plus·Jay L Mellies, Alex M S Barron
Sep 1, 2010·EcoSal Plus·Marcella PatrickTanya L Johnson
Jul 26, 2012·Biophysical Journal·Jocelyne Vreede, Remus Th Dame

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