ArticleNucleic acids research2003
Diversity of type II restriction endonucleases that require two DNA recognition sites.
Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 56 citations in OpenAlex.
- Bacterial restriction-modification systems: mechanisms of defense against phage infection.Biophysics reports · 2025Article
- Comprehensive Analysis of Antiphage Defense Mechanisms: Serovar-Specific Patterns.Antibiotics (Basel, Switzerland) · 2024Article
- Structures, activity and mechanism of the Type IIS restriction endonuclease PaqCI.Nucleic acids research · 2023Article
- A nucleotide-sensing endonuclease from the Gabija bacterial defense system.Nucleic acids research · 2021Article
- Modular prophage interactions driven by capsule serotype select for capsule loss under phage predation.The ISME journal · 2020Article
- 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
- Organization of the BcgI restriction-modification protein for the cleavage of eight phosphodiester bonds in DNA.Nucleic acids research · 2013Article
- A sequence-specific nicking endonuclease from streptomyces: purification, physical and catalytic properties.ISRN biochemistry · 2013Article
- DNA looping by FokI: the impact of synapse geometry on loop topology at varied site orientations.Nucleic acids research · 2012Article
- Illuminating the reaction pathway of the FokI restriction endonuclease by fluorescence resonance energy transfer.Nucleic acids research · 2012Article
- Visual analysis of concerted cleavage by type IIF restriction enzyme SfiI in subsecond time region.Biophysical journal · 2011Article
- On the role of DNA biomechanics in the regulation of gene expression.Journal of the Royal Society, Interface · 2011Review
- Concerted action at eight phosphodiester bonds by the BcgI restriction endonuclease.Nucleic acids research · 2011Article
- A putative mobile genetic element carrying a novel type IIF restriction-modification system (PluTI).Nucleic acids research · 2010Article
- Single-molecule dynamics of the DNA-EcoRII protein complexes revealed with high-speed atomic force microscopy.Biochemistry · 2009Article
- Differences between Ca2+ and Mg2+ in DNA binding and release by the SfiI restriction endonuclease: implications for DNA looping.Nucleic acids research · 2009Article
- Direct monitoring of allosteric recognition of type IIE restriction endonuclease EcoRII.The Journal of biological chemistry · 2008Article
- A switch in the mechanism of communication between the two DNA-binding sites in the SfiI restriction endonuclease.Journal of molecular biology · 2007Article
- DNA looping and translocation provide an optimal cleavage mechanism for the type III restriction enzymes.The EMBO journal · 2007Article
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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
Orthodox Type IIP restriction endonucleases, which are commonly used in molecular biological work, recognize a single palindromic DNA recognition sequence and cleave within or near this sequence. Several new studies have reported on structural and biochemical peculiarities of restriction endonucleases that differ from the orthodox in that they require two copies of a particular DNA recognition sequence to cleave the DNA. These two sites requiring restriction endonucleases belong to different subtypes of Type II restriction endonucleases, namely Types IIE, IIF and IIS. We compare enzymes of these three types with regard to their DNA recognition and cleavage properties. The simultaneous recognition of two identical DNA sites by these restriction endonucleases ensures that single unmethylated recognition sites do not lead to chromosomal DNA cleavage, and might reflect evolutionary connections to other DNA processing proteins that specifically function with two sites.
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