ArticleNucleic acids research2007
R.KpnI, an HNH superfamily REase, exhibits differential discrimination at non-canonical sequences in the presence of Ca2+ and Mg2+.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 27 citations in OpenAlex.
- Identification and characterization of a new HNH restriction endonuclease with unusual properties.Applied microbiology and biotechnology · 2023Article
- HK97 gp74 Possesses an α-Helical Insertion in the ββα Fold That Affects Its Metal Binding,Journal of bacteriology · 2020Article
- Calcium-driven DNA synthesis by a high-fidelity DNA polymerase.Nucleic acids research · 2017Article
- 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
- Increasing cleavage specificity and activity of restriction endonuclease KpnI.Nucleic acids research · 2013Article
- Diverse functions of restriction-modification systems in addition to cellular defense.Microbiology and molecular biology reviews : MMBR · 2013Review
- The protein gp74 from the bacteriophage HK97 functions as a HNH endonuclease.Protein science : a publication of the Protein Society · 2012Article
- Promiscuous restriction is a cellular defense strategy that confers fitness advantage to bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Homing endonucleases: from basics to therapeutic applications.Cellular and molecular life sciences : CMLS · 2010Review
- Cofactor requirement of HpyAV restriction endonuclease.PloS one · 2010Article
- Differences between Ca2+ and Mg2+ in DNA binding and release by the SfiI restriction endonuclease: implications for DNA looping.Nucleic acids research · 2009Article
- Evolution of sequence specificity in a restriction endonuclease by a point mutation.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Expression and purification of BmrI restriction endonuclease and its N-terminal cleavage domain variants.Protein expression and purification · 2008Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
KpnI REase recognizes palindromic sequence, GGTACC, and forms complex in the absence of divalent metal ions, but requires the ions for DNA cleavage. Unlike most other REases, R.KpnI shows promiscuous DNA cleavage in the presence of Mg2+. Surprisingly, Ca2+ suppresses the Mg2+-mediated promiscuous activity and induces high fidelity cleavage. To further analyze these unique features of the enzyme, we have carried out DNA binding and kinetic analysis. The metal ions which exhibit disparate pattern of DNA cleavage have no role in DNA recognition. The enzyme binds to both canonical and non-canonical DNA with comparable affinity irrespective of the metal ions used. Further, Ca2+-imparted exquisite specificity of the enzyme is at the level of DNA cleavage and not at the binding step. With the canonical oligonucleotides, the cleavage rate of the enzyme was comparable for both Mg2+- and Mn2+-mediated reactions and was about three times slower with Ca2+. The enzyme discriminates non-canonical sequences poorly from the canonical sequence in Mg2+-mediated reactions unlike any other Type II REases, accounting for the promiscuous behavior. R.KpnI, thus displays properties akin to that of typical Type II REases and also endonucleases with degenerate specificity in its DNA recognition and cleavage properties.
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