ArticleNucleic acids research2004
KpnI restriction endonuclease and methyltransferase exhibit contrasting mode of sequence recognition.
Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- Computational prediction resolves thousands of homooligomeric phage protein structures.bioRxiv : the preprint server for biology · 2026Article
- Macromolecular Crowding Enhances the Detection of DNA and Proteins by a Solid-State Nanopore.Nano letters · 2020Article
- Cleavage of adenine-modified functionalized DNA by type II restriction endonucleases.Nucleic acids research · 2009Article
- Highly efficient incorporation of the fluorescent nucleotide analogs tC and tCO by Klenow fragment.Nucleic acids research · 2009Article
- Mechanistic insights into replication termination as revealed by investigations of the Reb1-Ter3 complex of Schizosaccharomyces pombe.Molecular and cellular biology · 2008Article
- DNA bending in the mycobacterial plasmid pAL5000 origin-RepB complex.Journal of bacteriology · 2007Article
- Molecular architecture of a eukaryotic DNA replication terminus-terminator protein complex.Molecular and cellular biology · 2006Article
- Type II restriction endonuclease R.KpnI is a member of the HNH nuclease superfamily.Nucleic acids research · 2004Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The molecular basis of the interaction of KpnI restriction endonuclease (REase) and the corresponding methyltransferase (MTase) at their cognate recognition sequence is investigated using a range of footprinting techniques. DNase I protection analysis with the REase reveals the protection of a 14-18 bp region encompassing the hexanucleotide recognition sequence. The MTase, in contrast, protects a larger region. KpnI REase contacts two adjacent guanine residues and the single adenine residue in both the strands within the recognition sequence 5'-GGTACC-3', inferred by dimethylsulfate (DMS) protection, interference and missing nucleotide interference analysis. In contrast, KpnI MTase does not show elaborate base-specific contacts. Ethylation interference analysis also showed the differential interaction of REase and MTase with phosphate groups of three adjacent bases on both strands within the recognition sequence. The single thymine residue within the sequence is hyper- reactive to the permanganate oxidation, consistent with MTase-induced base flipping. The REase on the other hand does not show any major DNA distortion. The results demonstrate that the differences in the molecular interaction pattern of the two proteins at the same recognition sequence reflect the contrasting chemistry of DNA cleavage and methylation catalyzed by these two dissimilar enzymes, working in combination as constituents of a cellular defense strategy.
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