ArticleNucleic acids research2004
Type II restriction endonuclease R.KpnI is a member of the HNH nuclease superfamily.
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 46 papers.
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Who cites it
46 citing papers in PubMed, 82 citations in OpenAlex.
- DefensePredictor: A machine learning model to discover prokaryotic immune systems.Science (New York, N.Y.) · 2026Article
- Identification and characterization of a new HNH restriction endonuclease with unusual properties.Applied microbiology and biotechnology · 2023Article
- A DNase Type VI Secretion System Effector Requires Its MIX Domain for Secretion.Microbiology spectrum · 2022Article
- Crystal structure and DNA cleavage mechanism of the restriction DNA glycosylase R.CcoLI from Campylobacter coli.Scientific reports · 2021Article
- WSL9 Encodes an HNH Endonuclease Domain-Containing Protein that Is Essential for Early Chloroplast Development in Rice.Rice (New York, N.Y.) · 2020Article
- Distortion of double-stranded DNA structure by the binding of the restriction DNA glycosylase R.PabI.Nucleic acids research · 2020Article
- Structural and functional characterization of deep-sea thermophilic bacteriophage GVE2 HNH endonuclease.Scientific reports · 2017Article
- Tetrameric structure of the restriction DNA glycosylase R.PabI in complex with nonspecific double-stranded DNA.Scientific reports · 2016Article
- Members of the RAD52 Epistasis Group Contribute to Mitochondrial Homologous Recombination and Double-Strand Break Repair in Saccharomyces cerevisiae.PLoS genetics · 2015Article
- Mycobacterium tuberculosis RecG protein but not RuvAB or RecA protein is efficient at remodeling the stalled replication forks: implications for multiple mechanisms of replication restart in mycobacteria.The Journal of biological chemistry · 2015Article
- RNA aptamer inhibitors of a restriction endonuclease.Nucleic acids research · 2015Article
- Recognition and cleavage of 5-methylcytosine DNA by bacterial SRA-HNH proteins.Nucleic acids research · 2015Article
- Type II restriction endonucleases--a historical perspective and more.Nucleic acids research · 2014Review
- Elimination of inter-domain interactions increases the cleavage fidelity of the restriction endonuclease DraIII.Protein & cell · 2014Article
- HNH proteins are a widespread component of phage DNA packaging machines.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Increasing cleavage specificity and activity of restriction endonuclease KpnI.Nucleic acids research · 2013Article
- The role of the N-terminal loop in the function of the colicin E7 nuclease domain.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013Article
- Diverse functions of restriction-modification systems in addition to cellular defense.Microbiology and molecular biology reviews : MMBR · 2013Review
- Structural, functional and evolutionary relationships between homing endonucleases and proteins from their host organisms.Nucleic acids research · 2012Review
- The protein gp74 from the bacteriophage HK97 functions as a HNH endonuclease.Protein science : a publication of the Protein Society · 2012Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The restriction endonuclease (REase) R.KpnI is an orthodox Type IIP enzyme, which binds to DNA in the absence of metal ions and cleaves the DNA sequence 5'-GGTAC--C-3' in the presence of Mg2+ as shown generating 3' four base overhangs. Bioinformatics analysis reveals that R.KpnI contains a betabetaalpha-Me-finger fold, which is characteristic of many HNH-superfamily endonucleases, including homing endonuclease I-HmuI, structure-specific T4 endonuclease VII, colicin E9, sequence non-specific Serratia nuclease and sequence-specific homing endonuclease I-PpoI. According to our homology model of R.KpnI, D148, H149 and Q175 correspond to the critical D, H and N or H residues of the HNH nucleases. Substitutions of these three conserved residues lead to the loss of the DNA cleavage activity by R.KpnI, confirming their importance. The mutant Q175E fails to bind DNA at the standard conditions, although the DNA binding and cleavage can be rescued at pH 6.0, indicating a role for Q175 in DNA binding and cleavage. Our study provides the first experimental evidence for a Type IIP REase that does not belong to the PD...D/EXK superfamily of nucleases, instead is a member of the HNH superfamily.
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