ArticleNucleic acids research2013
Organization of the BcgI restriction-modification protein for the cleavage of eight phosphodiester bonds in DNA.
Article in Nucleic acids research, 2013. 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, 14 citations in OpenAlex.
- Biology of host-dependent restriction-modification in prokaryotes.EcoSal Plus · 2025Review
- Structure, subunit organization and behavior of the asymmetric Type IIT restriction endonuclease BbvCI.Nucleic acids research · 2019Article
- A model for the evolution of prokaryotic DNA restriction-modification systems based upon the structural malleability of Type I restriction-modification enzymes.Nucleic acids research · 2018Article
- Modification-dependent restriction endonuclease, MspJI, flips 5-methylcytosine out of the DNA helix.Nucleic acids research · 2014Article
- Structure of 5-hydroxymethylcytosine-specific restriction enzyme, AbaSI, in complex with DNA.Nucleic acids research · 2014Article
- Type II restriction endonucleases--a historical perspective and more.Nucleic acids research · 2014Review
- TstI, a Type II restriction-modification protein with DNA recognition, cleavage and methylation functions in a single polypeptide.Nucleic acids research · 2014Article
- Highlights of the DNA cutters: a short history of the restriction enzymes.Nucleic acids research · 2014Article
- Type I restriction enzymes and their relatives.Nucleic acids research · 2014Review
- Organization of the BcgI restriction-modification protein for the transfer of one methyl group to DNA.Nucleic acids research · 2013Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Type IIB restriction-modification systems, such as BcgI, feature a single protein with both endonuclease and methyltransferase activities. Type IIB nucleases require two recognition sites and cut both strands on both sides of their unmodified sites. BcgI cuts all eight target phosphodiester bonds before dissociation. The BcgI protein contains A and B polypeptides in a 2:1 ratio: A has one catalytic centre for each activity; B recognizes the DNA. We show here that BcgI is organized as A(2)B protomers, with B at its centre, but that these protomers self-associate to assemblies containing several A(2)B units. Moreover, like the well known FokI nuclease, BcgI bound to its site has to recruit additional protomers before it can cut DNA. DNA-bound BcgI can alternatively be activated by excess A subunits, much like the activation of FokI by its catalytic domain. Eight A subunits, each with one centre for nuclease activity, are presumably needed to cut the eight bonds cleaved by BcgI. Its nuclease reaction may thus involve two A(2)B units, each bound to a recognition site, with two more A(2)B units bridging the complexes by protein-protein interactions between the nuclease domains.
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