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Nucleic Acids Research 2005 33(21):6712-6722; doi:10.1093/nar/gki978
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Published online 27 November 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oxfordjournals.org

Article

Glucose repression of the Escherichia coli sdhCDAB operon, revisited: regulation by the CRP·cAMP complex

Tae-Wook Nam, Young-Ha Park, Hye-Jin Jeong, Sangryeol Ryu1 and Yeong-Jae Seok*

Laboratory of Macromolecular Interactions, Department of Biological Sciences and Institute of Microbiology, College of Natural Sciences, Seoul National University Seoul 151-742, Korea 1Department of Food and Animal Biotechnology, School of Agricultural Biotechnology and Center for Agricultural Biomaterials, Seoul National University Seoul 151-742, Korea

*To whom correspondence should be addressed. Tel: +82 2 880 8827; Fax: +82 2 888 4911; Email: yjseok{at}plaza.snu.ac.kr

Received October 24, 2005. Revised November 8, 2005. Accepted November 8, 2005.

Expression of the Escherichia coli sdhCDAB operon encoding the succinate dehydrogenase complex is regulated in response to growth conditions, such as anaerobiosis and carbon sources. An anaerobic repression of sdhCDAB is known to be mediated by the ArcB/A two-component system and the global Fnr anaerobic regulator. While the cAMP receptor protein (CRP) and Cra (formerly FruR) are known as key mediators of catabolite repression, they have been excluded from the glucose repression of the sdhCDAB operon. Although the glucose repression of sdhCDAB was reported to involve a mechanism dependent on the ptsG expression, the molecular mechanism underlying the glucose repression has never been clarified. In this study, we re-examined the mechanism of the sdhCDAB repression by glucose and found that CRP directly regulates expression of the sdhCDAB operon and that the glucose repression of this operon occurs in a cAMP-dependent manner. The levels of phosphorylated enzyme IIAGlc and intracellular cAMP on various carbon sources were proportional to the expression levels of sdhC-lacZ. Disruption of crp or cya completely abolished the glucose repression of sdhC-lacZ expression. Together with data showing correlation between the intracellular cAMP concentrations and the sdhC-lacZ expression levels in several mutants and wild type, in vitro transcription assays suggest that the decrease in the CRP·cAMP level in the presence of glucose is the major determinant of the glucose repression of the sdhCDAB operon.


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A. Nanchen, A. Schicker, O. Revelles, and U. Sauer
Cyclic AMP-Dependent Catabolite Repression Is the Dominant Control Mechanism of Metabolic Fluxes under Glucose Limitation in Escherichia coli
J. Bacteriol., April 1, 2008; 190(7): 2323 - 2330.
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