ArticleJournal of molecular biology2011
Structural analysis of a novel class of R-M controller proteins: C.Csp231I from
Article in Journal of molecular biology, 2011. 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, 12 citations in OpenAlex.
- Molecular basis for lethal cross-talk between two unrelated bacterial transcription factors - the regulatory protein of a restriction-modification system and the repressor of a defective prophage.Nucleic acids research · 2022Article
- I22: SAXS/WAXS beamline at Diamond Light Source - an overview of 10 years operation.Journal of synchrotron radiation · 2021Article
- Article
- Natural C-independent expression of restriction endonuclease in a C protein-associated 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
- BswR controls bacterial motility and biofilm formation in Pseudomonas aeruginosa through modulation of the small RNA rsmZ.Nucleic acids research · 2014Article
- Article
- Naturally-occurring, dually-functional fusions between restriction endonucleases and regulatory proteins.BMC evolutionary biology · 2013Article
- A novel restriction-modification system is responsible for temperature-dependent phage resistance in Listeria monocytogenes ECII.Applied and environmental microbiology · 2012Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Controller proteins play a key role in the temporal regulation of gene expression in bacterial restriction-modification (R-M) systems and are important mediators of horizontal gene transfer. They form the basis of a highly cooperative, concentration-dependent genetic switch involved in both activation and repression of R-M genes. Here we present biophysical, biochemical, and high-resolution structural analysis of a novel class of controller proteins, exemplified by C.Csp231I. In contrast to all previously solved C-protein structures, each protein subunit has two extra helices at the C-terminus, which play a large part in maintaining the dimer interface. The DNA binding site of the protein is also novel, having largely AAAA tracts between the palindromic recognition half-sites, suggesting tight bending of the DNA. The protein structure shows an unusual positively charged surface that could form the basis for wrapping the DNA completely around the C-protein dimer.
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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.