ArticleNucleic acids research2008
Tetrameric restriction enzymes: expansion to the GIY-YIG nuclease family.
Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 26 citations in OpenAlex.
- Bacterial restriction-modification systems: mechanisms of defense against phage infection.Biophysics reports · 2025Article
- Characterization of a Novel N4-Methylcytosine Restriction-Modification System inInternational journal of molecular sciences · 2024Article
- Type II Restriction-Modification System fromPathogens (Basel, Switzerland) · 2020Article
- Structure, subunit organization and behavior of the asymmetric Type IIT restriction endonuclease BbvCI.Nucleic acids research · 2019Article
- UbaLAI is a monomeric Type IIE restriction enzyme.Nucleic acids research · 2017Article
- CgII cleaves DNA using a mechanism distinct from other ATP-dependent restriction endonucleases.Nucleic acids research · 2017Article
- Type II restriction endonucleases--a historical perspective and more.Nucleic acids research · 2014Review
- Hpy188I-DNA pre- and post-cleavage complexes--snapshots of the GIY-YIG nuclease mediated catalysis.Nucleic acids research · 2011Article
- Divalent metal ion differentially regulates the sequential nicking reactions of the GIY-YIG homing endonuclease I-BmoI.PloS one · 2011Article
- DNA synapsis through transient tetramerization triggers cleavage by Ecl18kI restriction enzyme.Nucleic acids research · 2010Article
- Folding, DNA recognition, and function of GIY-YIG endonucleases: crystal structures of R.Eco29kI.Structure (London, England : 1993) · 2010Article
- A unified genetic, computational and experimental framework identifies functionally relevant residues of the homing endonuclease I-BmoI.Nucleic acids research · 2010Article
- Cofactor requirement of HpyAV restriction endonuclease.PloS one · 2010Article
- Bacteriophage T4 endonuclease II, a promiscuous GIY-YIG nuclease, binds as a tetramer to two DNA substrates.Nucleic acids research · 2009Article
- Amino acid residues in the GIY-YIG endonuclease II of phage T4 affecting sequence recognition and binding as well as catalysis.Journal of bacteriology · 2008Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The GIY-YIG nuclease domain was originally identified in homing endonucleases and enzymes involved in DNA repair and recombination. Many of the GIY-YIG family enzymes are functional as monomers. We show here that the Cfr42I restriction endonuclease which belongs to the GIY-YIG family and recognizes the symmetric sequence 5'-CCGC/GG-3' ('/' indicates the cleavage site) is a tetramer in solution. Moreover, biochemical and kinetic studies provided here demonstrate that the Cfr42I tetramer is catalytically active only upon simultaneous binding of two copies of its recognition sequence. In that respect Cfr42I resembles the homotetrameric Type IIF restriction enzymes that belong to the distinct PD-(E/D)XK nuclease superfamily. Unlike the PD-(E/D)XK enzymes, the GIY-YIG nuclease Cfr42I accommodates an extremely wide selection of metal-ion cofactors, including Mg2+, Mn2+, Co2+, Zn2+, Ni2+, Cu2+ and Ca2+. To our knowledge, Cfr42I is the first tetrameric GIY-YIG family enzyme. Similar structural arrangement and phenotypes displayed by restriction enzymes of the PD-(E/D)XK and GIY-YIG nuclease families point to the functional significance of tetramerization.
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