The DOI matches its Crossref record; 269 of the 269 references it cites were found in a registry or an index.
The TetR Family of Regulators
Open accessAbstract
SUMMARY: The most common prokaryotic signal transduction mechanisms are the one-component systems in which a single polypeptide contains both a sensory domain and a DNA-binding domain. Among the >20 classes of one-component systems, the TetR family of regulators (TFRs) are widely associated with antibiotic resistance and the regulation of genes encoding small-molecule exporters. However, TFRs play a much broader role, controlling genes involved in metabolism, antibiotic production, quorum sensing, and many other aspects of prokaryotic physiology. There are several well-established model systems for understanding these important proteins, and structural studies have begun to unveil the mechanisms by which they bind DNA and recognize small-molecule ligands. The sequences for more than 200,000 TFRs are available in the public databases, and genomics studies are identifying their target genes. Three-dimensional structures have been solved for close to 200 TFRs. Comparison of these structures reveals a common overall architecture of nine conserved α helices. The most important open question concerning TFR biology is the nature and diversity of their ligands and how these relate to the biochemical processes under their control.
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Metadata
- Authors
- Cuthbertson, L., & Nodwell, J. R.
- Venue
- Microbiology and Molecular Biology Reviews
- Publisher
- American Society for Microbiology
- Published
- 2013-09
- Volume
- 77
- Issue
- 3
- Pages
- 440-475
- ISSN
- 1092-2172 (ISSN-L)
- 1098-5557
- OpenAlex
- W2102964870
- Cited by
- 554
- References
- 269
- FWCI
- 2.81
- Type
- journal article
- Language
- en
- Open access
- green
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