Evidence map›Paper›PMID 15944459›Full record

ReviewMicrobiology and molecular biology reviews : MMBR2005

The TetR family of transcriptional repressors.

Juan L Ramos, Manuel Martínez-Bueno, Antonio J Molina-Henares, Wilson Terán, Kazuya Watanabe, Xiaodong Zhang, María Trinidad Gallegos, Richard Brennan, Raquel Tobes

Abstract readComparative StudyReview
In one paragraph

Review in Microbiology and molecular biology reviews : MMBR, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 573 papers.

0numbers the graph read from it
0cells of the map it votes in
573citing papers in PubMed
37.5field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

573 citing papers in PubMed, 1,112 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

513 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 5 institutions in 4 countries.

Juan L RamosDepartment of Plant Biochemistry and Molecular and Cellular Biology, Estación Experimental del Zaidín, Consejo Superior de Investigaciones Cientificas, Granada, Spain. jlramos@eez.csic.es
Manuel Martínez-Bueno
Antonio J Molina-Henares
Wilson Terán
Kazuya Watanabe
Xiaodong Zhang
María Trinidad Gallegos
Richard Brennan
Raquel Tobes
Consejo Superior de Investigaciones Científicas · ESEstación Experimental del Zaidín · ESImperial College London · GBIwate Prefectural Kamaishi Hospital · JPOregon Health & Science University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

Transcription, GeneticAdaptation, PhysiologicalAmino Acid SequenceBacteriaBacterial ProteinsModels, MolecularMolecular Sequence DataRepressor ProteinsSequence AlignmentSignal TransductionTetracyclineTetracycline ResistanceBacterial ProteinsEthR protein, Mycobacterium tuberculosisQacR protein, Staphylococcus aureusRepressor ProteinsTetracyclinetetracycline resistance-encoding transposon repressor protein

Identifiers

PMID15944459
PMCPMC1197418
OpenAlexW2171535756

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.