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AraC protein, regulation of the l-arabinose operon in Escherichia coli, and the light switch mechanism of AraC action.

Robert Schleif

Journal: FEMS microbiology reviews 2011;34(5):779-96

PMID: 20491933

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Abstract

This review covers the physiological aspects of regulation of the arabinose operon in Escherichia coli and the physical and regulatory properties of the operon's controlling gene, araC. It also describes the light switch mechanism as an explanation for many of the protein's properties. Although many thousands of homologs of AraC exist and regulate many diverse operons in response to many different inducers or physiological states, homologs that regulate arabinose-catabolizing genes in response to arabinose were identified. The sequence similarities among them are discussed in light of the known structure of the dimerization and DNA-binding domains of AraC.

Address: Biology Department, Johns Hopkins University, 3400 N. Charles St., Baltimore, MD 21218, USA. [email protected]
DOI: 10.1111/j.1574-6976.2010.00226.x

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MeSH Terms: Allosteric Site, Amino Acid Sequence, AraC Transcription Factor, Arabinose, DNA, Bacterial, Escherichia coli, Escherichia coli Proteins, Fluorescence, Gene Expression Regulation, Bacterial, Models, Molecular, Molecular Sequence Data, Operon, Protein Binding, Protein Multimerization, Protein Structure, Tertiary, Sequence Alignment, Trans-Activators
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