ArticleNucleic acids research2012
Recognition of dual symmetry by the controller protein C.Esp1396I based on the structure of the transcriptional activation complex.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 13 citations in OpenAlex.
- Regulation of a phage defence island by RptR, a novel repressor that controls restriction-modification systems in diverse bacteria.Nucleic acids research · 2025Article
- Alignment of major-groove hydrogen bond arrays uncovers shared information between different DNA sequences that bind the same protein.NAR genomics and bioinformatics · 2022Article
- From biophysics to 'omics and systems biology.European biophysics journal : EBJ · 2019Review
- Effects of Population Dynamics on Establishment of a Restriction-Modification System in a Bacterial Host.Molecules (Basel, Switzerland) · 2019Article
- Widespread anti-CRISPR proteins in virulent bacteriophages inhibit a range of Cas9 proteins.Nature communications · 2018Article
- Structural analysis of DNA binding by C.Csp231I, a member of a novel class of R-M controller proteins regulating gene expression.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Article
- Highlights of the DNA cutters: a short history of the restriction enzymes.Nucleic acids research · 2014Article
- Structural analysis of DNA-protein complexes regulating the restriction-modification system Esp1396I.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- The structural basis of differential DNA sequence recognition by restriction-modification controller proteins.Nucleic acids research · 2012Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The controller protein C.Esp1396I regulates the timing of gene expression of the restriction-modification (RM) genes of the RM system Esp1396I. The molecular recognition of promoter sequences by such transcriptional regulators is poorly understood, in part because the DNA sequence motifs do not conform to a well-defined symmetry. We report here the crystal structure of the controller protein bound to a DNA operator site. The structure reveals how two different symmetries within the operator are simultaneously recognized by the homo-dimeric protein, underpinned by a conformational change in one of the protein subunits. The recognition of two different DNA symmetries through movement of a flexible loop in one of the protein subunits may represent a general mechanism for the recognition of pseudo-symmetric DNA sequences.
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