ArticleGenes & development2010
Crystal structure of TtgV in complex with its DNA operator reveals a general model for cooperative DNA binding of tetrameric gene regulators.
Article in Genes & development, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Tuning the performance of a TphR-based terephthalate biosensor with a design of experiments approach.Metabolic engineering communications · 2024Article
- Structural insights into CodY activation and DNA recognition.Nucleic acids research · 2023Article
- Investigating a putative transcriptional regulatory protein encoded by Rv1719 gene of Mycobacterium tuberculosis.The protein journal · 2022Article
- Comparative Analysis of the IclR-Family of Bacterial Transcription Factors and Their DNA-Binding Motifs: Structure, Positioning, Co-Evolution, Regulon Content.Frontiers in microbiology · 2021Article
- Molecular control of gene expression byThe Journal of biological chemistry · 2018Article
- Studying protein-DNA interactions using atomic force microscopy.Seminars in cell & developmental biology · 2018Review
- A microbial sensor for organophosphate hydrolysis exploiting an engineered specificity switch in a transcription factor.Nucleic acids research · 2016Article
- TrmBL2 from Pyrococcus furiosus Interacts Both with Double-Stranded and Single-Stranded DNA.PloS one · 2016Article
- Crystal structure of Hop2-Mnd1 and mechanistic insights into its role in meiotic recombination.Nucleic acids research · 2015Article
- Structural and functional basis of transcriptional regulation by TetR family protein CprB from S. coelicolor A3(2).Nucleic acids research · 2014Article
- Insight into the cooperative DNA binding of the O⁶-alkylguanine DNA alkyltransferase.DNA repair · 2014Review
- Identification of new residues involved in intramolecular signal transmission in a prokaryotic transcriptional repressor.Journal of bacteriology · 2014Article
- Structures of the Porphyromonas gingivalis OxyR regulatory domain explain differences in expression of the OxyR regulon in Escherichia coli and P. gingivalis.Acta crystallographica. Section D, Biological crystallography · 2013Article
- In vivo analysis of DNA binding and ligand interaction of BlcR, an IclR-type repressor from Agrobacterium tumefaciens.Microbiology (Reading, England) · 2013Article
- GenR, an IclR-type regulator, activates and represses the transcription of gen genes involved in 3-hydroxybenzoate and gentisate catabolism in Corynebacterium glutamicum.Journal of bacteriology · 2013Article
- Intramolecular signal transmission in a tetrameric repressor of the IclR family.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Structural basis of cooperative DNA recognition by the plasmid conjugation factor, TraM.Nucleic acids research · 2011Article
- Light-dependent gene regulation by a coenzyme B12-based photoreceptor.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
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10 authors.
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Abstract
The majority of bacterial gene regulators bind as symmetric dimers to palindromic DNA operators of 12-20 base pairs (bp). Multimeric forms of proteins, including tetramers, are able to recognize longer operator sequences in a cooperative manner, although how this is achieved is not well understood due to the lack of complete structural information. Models, instead of structures, of complete tetrameric assembly on DNA exist in literature. Here we present the crystal structures of the multidrug-binding protein TtgV, a gene repressor that controls efflux pumps, alone and in complex with a 42-bp DNA operator containing two TtgV recognition sites at 2.9 Å and 3.4 Å resolution. These structures represent the first full-length functional tetrameric protein in complex with its intact DNA operator containing two continuous recognition sites. TtgV binds to its DNA operator as a highly asymmetric tetramer and induces considerable distortions in the DNA, resulting in a 60° bend. Upon binding to its operator, TtgV undergoes large conformational changes at the monomeric, dimeric, and tetrameric levels. The structures here reveal a general model for cooperative DNA binding of tetrameric gene regulators and provide a structural basis for a large body of biochemical data and a reinterpretation of previous models for tetrameric gene regulators derived from partial structural data.
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