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Structure and function of the LysR-type transcriptional regulator (LTTR) family proteins
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...
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Published in: | Microbiology (Society for General Microbiology) 2008-12, Vol.154 (12), p.3609-3623 |
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Main Authors: | , |
Format: | Article |
Language: | English |
Subjects: | |
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Online Access: | Get full text |
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Summary: | 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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ISSN: | 1350-0872 1465-2080 |
DOI: | 10.1099/mic.0.2008/022772-0 |