ArticleActa crystallographica. Section F, Structural biology and crystallization communications2013
Structural analysis of DNA-protein complexes regulating the restriction-modification system Esp1396I.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Alignment of major-groove hydrogen bond arrays uncovers shared information between different DNA sequences that bind the same protein.NAR genomics and bioinformatics · 2022Article
- 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
- Effects of Population Dynamics on Establishment of a Restriction-Modification System in a Bacterial Host.Molecules (Basel, Switzerland) · 2019Article
- 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
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Authors and funding
6 authors.
Funding
Abstract
The controller protein of the type II restriction-modification (RM) system Esp1396I binds to three distinct DNA operator sequences upstream of the methyltransferase and endonuclease genes in order to regulate their expression. Previous biophysical and crystallographic studies have shown molecular details of how the controller protein binds to the operator sites with very different affinities. Here, two protein-DNA co-crystal structures containing portions of unbound DNA from native operator sites are reported. The DNA in both complexes shows significant distortion in the region between the conserved symmetric sequences, similar to that of a DNA duplex when bound by the controller protein (C-protein), indicating that the naked DNA has an intrinsic tendency to bend when not bound to the C-protein. Moreover, the width of the major groove of the DNA adjacent to a bound C-protein dimer is observed to be significantly increased, supporting the idea that this DNA distortion contributes to the substantial cooperativity found when a second C-protein dimer binds to the operator to form the tetrameric repression complex.
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