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Microbiology 154 (2008), 3609-3623; DOI  10.1099/mic.0.2008/022772-0IMMEDIATE OPEN ACCESS ARTICLE
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Microbiology 154 (2008), 3609-3623; DOI  10.1099/mic.0.2008/022772-0
© 2008 Society for General Microbiology

Review

Structure and function of the LysR-type transcriptional regulator (LTTR) family proteins

Sarah E. Maddocks1 and Petra C. F. Oyston2

1 Department of Oral and Dental Science, University of Bristol, Lower Maudlin Street, Bristol BS1 2LY, UK
2 Biomedical Sciences, DSTL Porton Down, Salisbury SP4 0JQ, UK

Correspondence
Sarah E. Maddocks
sarah.maddocks{at}bristol.ac.uk

The LysR family of transcriptional regulators represents the most abundant type of transcriptional regulator in the prokaryotic kingdom. Members of this family have a conserved structure with an N-terminal DNA-binding helix–turn–helix motif and a C-terminal co-inducer-binding domain. Despite considerable conservation both structurally and functionally, LysR-type transcriptional regulators (LTTRs) regulate a diverse set of genes, including those involved in virulence, metabolism, quorum sensing and motility. Numerous structural and transcriptional studies of members of the LTTR family are helping to unravel a compelling paradigm that has evolved from the original observations and conclusions that were made about this family of transcriptional regulators.

Abbreviations: ABS, activation binding site; DBD, DNA-binding domain; HTH, helix–turn–helix; wHTH, winged-HTH; LTTR, LysR-type transcriptional regulator; RBS, regulatory binding site




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