ArticleNucleic acids research2012
The structural basis of differential DNA sequence recognition by restriction-modification controller proteins.
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 15 papers.
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Who cites it
15 citing papers in PubMed, 21 citations in OpenAlex.
- Biology of host-dependent restriction-modification in prokaryotes.EcoSal Plus · 2025Review
- Nonlinear regulatory dynamics of bacterial restriction-modification systems modulates horizontal gene transfer susceptibility.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
- Article
- Transcriptome analyses of cells carrying the Type II Csp231I restriction-modification system reveal cross-talk between two unrelated transcription factors: C protein and the Rac prophage repressor.Nucleic acids research · 2019Article
- Structural characterization of Class 2 OLD family nucleases supports a two-metal catalysis mechanism for cleavage.Nucleic acids research · 2019Article
- The structure of a polygamous repressor reveals how phage-inducible chromosomal islands spread in nature.Nature communications · 2019Article
- Kinetic Basis of the Bifunctionality of SsoII DNA Methyltransferase.Molecules (Basel, Switzerland) · 2018Article
- Understanding key features of bacterial restriction-modification systems through quantitative modeling.BMC systems biology · 2017Article
- Temporal dynamics of methyltransferase and restriction endonuclease accumulation in individual cells after introducing a restriction-modification system.Nucleic acids research · 2016Article
- 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
- Naturally-occurring, dually-functional fusions between restriction endonucleases and regulatory proteins.BMC evolutionary biology · 2013Article
- Structural analysis of DNA-protein complexes regulating the restriction-modification system Esp1396I.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
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Abstract
Controller (C) proteins regulate the expression of restriction-modification (RM) genes in a wide variety of RM systems. However, the RM system Esp1396I is of particular interest as the C protein regulates both the restriction endonuclease (R) gene and the methyltransferase (M) gene. The mechanism of this finely tuned genetic switch depends on differential binding affinities for the promoters controlling the R and M genes, which in turn depends on differential DNA sequence recognition and the ability to recognize dual symmetries. We report here the crystal structure of the C protein bound to the M promoter, and compare the binding affinities for each operator sequence by surface plasmon resonance. Comparison of the structure of the transcriptional repression complex at the M promoter with that of the transcriptional activation complex at the R promoter shows how subtle changes in protein-DNA interactions, underpinned by small conformational changes in the protein, can explain the molecular basis of differential regulation of gene expression.
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