ArticleNucleic acids research2009
Crystal structure of KorA bound to operator DNA: insight into repressor cooperation in RP4 gene regulation.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 30 citations in OpenAlex.
- KorB switching from DNA-sliding clamp to repressor mediates long-range gene silencing in a multi-drug resistance plasmid.Nature microbiology · 2025Article
- Inhibition of Plasmid Conjugation inInternational journal of molecular sciences · 2023Article
- Structural basis of direct and inverted DNA sequence repeat recognition by helix-turn-helix transcription factors.Nucleic acids research · 2022Article
- Nonnutritive sweeteners can promote the dissemination of antibiotic resistance through conjugative gene transfer.The ISME journal · 2021Article
- Deciphering the regulon of a GntR family regulator via transcriptome and ChIP-exo analyses and its contribution to virulence in Xanthomonas citri.Molecular plant pathology · 2017Article
- Flexibility of KorA, a plasmid-encoded, global transcription regulator, in the presence and the absence of its operator.Nucleic acids research · 2016Article
- GntR Family of Bacterial Transcription Factors and Their DNA Binding Motifs: Structure, Positioning and Co-Evolution.PloS one · 2015Article
- Re-visiting protein-centric two-tier classification of existing DNA-protein complexes.BMC bioinformatics · 2012Article
- Origins of specificity in protein-DNA recognition.Annual review of biochemistry · 2010Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
KorA is a global repressor in RP4 which regulates cooperatively the expression of plasmid genes whose products are involved in replication, conjugative transfer and stable inheritance. The structure of KorA bound to an 18-bp DNA duplex that contains the symmetric operator sequence and incorporates 5-bromo-deoxyuridine nucleosides has been determined by multiple-wavelength anomalous diffraction phasing at 1.96-A resolution. KorA is present as a symmetric dimer and contacts DNA via a helix-turn-helix motif. Each half-site of the symmetric operator DNA binds one copy of the protein in the major groove. As confirmed by mutagenesis, recognition specificity is based on two KorA side chains forming hydrogen bonds to four bases within each operator half-site. KorA has a unique dimerization module shared by the RP4 proteins TrbA and KlcB. We propose that these proteins cooperate with the global RP4 repressor KorB in a similar manner via this dimerization module and thus regulate RP4 inheritance.
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Registered trials
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.