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Microbiology 147 (2001), 2215-2221
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Microbiology (2001), 147, 2215-2221.
© 2001 Society for General Microbiology

Genetics and Molecular Biology

GcvR interacts with GcvA to inhibit activation of the Escherichia coli glycine cleavage operon

Angela C. Ghrist1, Gary Heil1 and George V. Stauffer1

Department of Microbiology, The University of Iowa, Iowa City, IA 52242, USA1

Author for correspondence: George V. Stauffer. Tel: +1 319 335 7791. Fax: +1 319 335 9006. e-mail: george-stauffer{at}uiowa.edu

The Escherichia coli glycine cleavage enzyme system, encoded by the gcvTHP operon, catalyses the oxidative cleavage of glycine to CO2, NH3 and a one-carbon methylene group. Transcription of the gcv operon is positively regulated by GcvA and negatively regulated by GcvA and GcvR. Using a LexA-based system for analysing protein heterodimerization, it is shown that GcvR interacts directly with GcvA in vivo to repress gcvTHP expression. Several mutations in either gcvA or gcvR that result in a loss of gcv repression also result in a loss of GcvA/GcvR heterodimerization. Finally, it is shown that the C-terminal half of GcvA is involved in its interaction with GcvR, whilst the entire GcvR protein appears to be necessary for heterodimerization.

Keywords: gcvTHP, repressor, activator, repression, antiactivation

Abbreviations: AP, ampicillin; DBD, DNA-binding domain; gcv, gcvTHP; TC, tetracycline; TPEG, phenylethyl-ß-D-thiogalactoside




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