ArticleNucleic acids research2004
Analysis of the LAGLIDADG interface of the monomeric homing endonuclease I-DmoI.
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 17 papers.
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Who cites it
17 citing papers in PubMed.
- Computational prediction resolves thousands of homooligomeric phage protein structures.bioRxiv : the preprint server for biology · 2026Article
- Active site residue identity regulates cleavage preference of LAGLIDADG homing endonucleases.Nucleic acids research · 2018Article
- The Structural Basis of Asymmetry in DNA Binding and Cleavage as Exhibited by the I-SmaMI LAGLIDADG Meganuclease.Journal of molecular biology · 2016Article
- Engineering a Nickase on the Homing Endonuclease I-DmoI Scaffold.The Journal of biological chemistry · 2015Article
- Control of catalytic efficiency by a coevolving network of catalytic and noncatalytic residues.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Article
- Homing endonucleases: from genetic anomalies to programmable genomic clippers.Methods in molecular biology (Clifton, N.J.) · 2014Review
- Engineering domain fusion chimeras from I-OnuI family LAGLIDADG homing endonucleases.Nucleic acids research · 2012Article
- Homing endonucleases: from microbial genetic invaders to reagents for targeted DNA modification.Structure (London, England : 1993) · 2011Review
- Natural and engineered nicking endonucleases--from cleavage mechanism to engineering of strand-specificity.Nucleic acids research · 2011Review
- Generation of single-chain LAGLIDADG homing endonucleases from native homodimeric precursor proteins.Nucleic acids research · 2009Article
- Generation of a nicking enzyme that stimulates site-specific gene conversion from the I-AniI LAGLIDADG homing endonuclease.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Optimization of in vivo activity of a bifunctional homing endonuclease and maturase reverses evolutionary degradation.Nucleic acids research · 2009Article
- Computer design of obligate heterodimer meganucleases allows efficient cutting of custom DNA sequences.Nucleic acids research · 2008Article
- Rational design of a chimeric endonuclease targeted to NotI recognition site.Protein engineering, design & selection : PEDS · 2007Article
- A combinatorial approach to create artificial homing endonucleases cleaving chosen sequences.Nucleic acids research · 2006Article
- I-ApeKI [corrected]: a novel intron-encoded LAGLIDADG homing endonuclease from the archaeon, Aeropyrum pernix K1.Nucleic acids research · 2005Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The general structural fold of the LAGLIDADG endonuclease family consists of two similar alpha/beta domains (alphabetabetaalphabetabetaalpha) that assemble either as homodimers or monomers with the domains related by pseudo-two-fold symmetry. At the center of this symmetry is the closely packed LAGLIDADG two-helix bundle that forms the main inter- or intra-molecular contact region between the domains of single- or double-motif proteins, respectively. In this work, we further examine the role of the LAGLIDADG residues involved in the helix-helix interaction. The interchangeability of the LAGLIDADG helix interaction was explored by grafting interfacial residues from the homodimeric I-CreI into the corresponding positions in the monomeric I-DmoI. The resulting LAGLIDADG exchange mutant is partially active, preferring to nick dsDNA rather than making the customary double-strand break. A series of partial revertants within the mutated LAGLIDADG region are shown to restore cleavage activity to varying degrees resulting in one I-DmoI mutant that is more active than wild-type I-DmoI. The phenotype of some of these mutants was reconciled on the basis of similarity to the GxxxG helix interaction found in transmembrane proteins. Additionally, a split variant of I-DmoI was created, demonstrating that the LAGLIDADG helices of I-DmoI are capable of forming and maintaining the protein-protein interface in trans to create an active heterodimer.
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