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PMID: 15944459 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Review

The TetR family of transcriptional repressors.

Microbiology and molecular biology reviews : MMBR ·Vol. 69 ·No. 2 ·2005-06-00 ·Pages 326-56

Ramos JL, Martínez-Bueno M, Molina-Henares AJ, Terán W, Watanabe K, Zhang X, Gallegos MT, Brennan R, Tobes R

Abstract

We have developed a general profile for the proteins of the TetR family of repressors. The stretch that best defines the profile of this family is made up of 47 amino acid residues that correspond to the helix-turn-helix DNA binding motif and adjacent regions in the three-dimensional structures of TetR, QacR, CprB, and EthR, four family members for which the function and three-dimensional structure are known. We have detected a set of 2,353 nonredundant proteins belonging to this family by screening genome and protein databases with the TetR profile. Proteins of the TetR family have been found in 115 genera of gram-positive, alpha-, beta-, and gamma-proteobacteria, cyanobacteria, and archaea. The set of genes they regulate is known for 85 out of the 2,353 members of the family. These proteins are involved in the transcriptional control of multidrug efflux pumps, pathways for the biosynthesis of antibiotics, response to osmotic stress and toxic chemicals, control of catabolic pathways, differentiation processes, and pathogenicity. The regulatory network in which the family member is involved can be simple, as in TetR (i.e., TetR bound to the target operator represses tetA transcription and is released in the presence of tetracycline), or more complex, involving a series of regulatory cascades in which either the expression of the TetR family member is modulated by another regulator or the TetR family member triggers a cell response to react to environmental insults. Based on what has been learned from the cocrystals of TetR and QacR with their target operators and from their three-dimensional structures in the absence and in the presence of ligands, and based on multialignment analyses of the conserved stretch of 47 amino acids in the 2,353 TetR family members, two groups of residues have been identified. One group includes highly conserved positions involved in the proper orientation of the helix-turn-helix motif and hence seems to play a structural role. The other set of less conserved residues are involved in establishing contacts with the phosphate backbone and target bases in the operator. Information related to the TetR family of regulators has been updated in a database that can be accessed at www.bactregulators.org.

MeSH Terms
Adaptation, Physiological/genetics Amino Acid Sequence Bacteria/drug effects,genetics Bacterial Proteins/chemistry,genetics,metabolism Models, Molecular Molecular Sequence Data Repressor Proteins/chemistry,genetics,metabolism Sequence Alignment Signal Transduction Tetracycline/pharmacology Tetracycline Resistance Transcription, Genetic
Chemicals
Bacterial Proteins EthR protein, Mycobacterium tuberculosis QacR protein, Staphylococcus aureus Repressor Proteins tetracycline resistance-encoding transposon repressor protein Tetracycline
Authors & Affiliations
9 authors, click to expand affiliations / ORCID
Ramos Juan L
Department of Plant Biochemistry and Molecular and Cellular Biology, Estación Experimental del Zaidín, Consejo Superior de Investigaciones Cientificas, Granada, Spain. jlramos@eez.csic.es
Martínez-Bueno Manuel
Molina-Henares Antonio J
Terán Wilson
Watanabe Kazuya
Zhang Xiaodong
Gallegos María Trinidad
Brennan Richard
Tobes Raquel
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Article Info
Journal
Microbiology and molecular biology reviews : MMBR
Abbr.
Microbiol Mol Biol Rev
ISSN
1092-2172
DOI
10.1128/MMBR.69.2.326-356.2005
Email
jlramos@eez.csic.es
Published
2005-06-00
Pages
326-56
Language
English
Region
United States
NLM ID
9706653
PMCID
PMC1197418
Subset
IM
External Links
PubMed source DOI: 10.1128/MMBR.69.2.326-356.2005 PMC Full Text View journal details
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