ArticleProceedings of the National Academy of Sciences of the United States of America2002
Zinc finger as distance determinant in the flexible linker of intron endonuclease I-TevI.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. 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, 49 citations in OpenAlex.
- Modular determinants of cleavage preference in GIY-YIG nucleases revealed by block-based DNA shuffling and directed evolution.Nucleic acids research · 2026Article
- A buffer-tuning strategy to profile domain-specific activity of chimeric I-TevI/CRISPR gene editors in vitro.Scientific reports · 2025Article
- Structure and RNA-binding of the helically extended Roquin CCCH-type zinc finger.Nucleic acids research · 2024Article
- A Photoresponsive Homing Endonuclease for Programmed DNA Cleavage.ACS synthetic biology · 2024Article
- Biasing genome-editing events toward precise length deletions with an RNA-guided TevCas9 dual nuclease.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Perpetuating the homing endonuclease life cycle: identification of mutations that modulate and change I-TevI cleavage preference.Nucleic acids research · 2016Article
- The I-TevI nuclease and linker domains contribute to the specificity of monomeric TALENs.G3 (Bethesda, Md.) · 2014Article
- The monomeric GIY-YIG homing endonuclease I-BmoI uses a molecular anchor and a flexible tether to sequentially nick DNA.Nucleic acids research · 2013Article
- Compact designer TALENs for efficient genome engineering.Nature communications · 2013Article
- Monomeric site-specific nucleases for genome editing.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Redox-responsive zinc finger fidelity switch in homing endonuclease and intron promiscuity in oxidative stress.Current biology : CB · 2011Article
- Divalent metal ion differentially regulates the sequential nicking reactions of the GIY-YIG homing endonuclease I-BmoI.PloS one · 2011Article
- Mobile DNA elements in T4 and related phages.Virology journal · 2010Review
- A unified genetic, computational and experimental framework identifies functionally relevant residues of the homing endonuclease I-BmoI.Nucleic acids research · 2010Article
- Homing endonucleases: from basics to therapeutic applications.Cellular and molecular life sciences : CMLS · 2010Review
- Scientific serendipity initiates an intron odyssey.The Journal of biological chemistry · 2009Article
- Role of the interdomain linker in distance determination for remote cleavage by homing endonuclease I-TevI.Journal of molecular biology · 2008Article
- Phage T4 SegB protein is a homing endonuclease required for the preferred inheritance of T4 tRNA gene region occurring in co-infection with a related phage.Nucleic acids research · 2008Article
- Analysis of the zinc finger domain of TnpA, a DNA targeting protein encoded by mobilizable transposon Tn4555.Plasmid · 2007Article
- Thermodynamics of DNA target site recognition by homing endonucleases.Nucleic acids research · 2007Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
I-TevI, the phage T4 td intron-encoded endonuclease, recognizes a lengthy DNA target and initiates intron mobility by introducing a double-strand break in the homing site. The enzyme uses both sequence and distance determinants to cleave the DNA 23-25 bp upstream of the intron insertion site. I-TevI consists of an N-terminal catalytic domain and a C-terminal DNA-binding domain separated by a long, flexible linker. The DNA-binding domain consists of three subdomains: a zinc finger, a minor-groove binding alpha-helix, and a helix-turn-helix. In this study, a mutational analysis was undertaken to assess the roles of these subdomains in substrate binding and cleavage. Surprisingly, the zinc finger is not required for DNA binding or catalysis. Rather, the zinc finger is a component of the linker and directs the catalytic domain to cleave the homing site at a fixed distance from the intron insertion site. When the cleavage site (CS) is shifted outside a given range, wild-type I-TevI defaults to the fixed distance, whereas zinc-finger mutants have lost the distance determinant and search out the displaced cleavage sequences. Although counterintuitive, a protein containing a 19-aa deletion of the zinc finger can extend further than can wild-type I-TevI to cleave a distant CS sequence, and a Cys-to-Ala mutant of the ligands for zinc, nominally a longer protein, can retract to cleave at a closer CS sequence. Models are presented for the novel function of the zinc finger, as a molecular constraint, whereby intramolecular protein-protein interactions position the catalytic domain by "catalytic clamp" and/or "linker-organizer" mechanisms.
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