ArticleNucleic acids research2014
The Mus81-Mms4 structure-selective endonuclease requires nicked DNA junctions to undergo conformational changes and bend its DNA substrates for cleavage.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Concurrent D-loop cleavage by Mus81 and Yen1 yields half-crossover precursors.Nucleic acids research · 2024Article
- Making Choices: DNA Replication Fork Recovery Mechanisms.Seminars in cell & developmental biology · 2021Review
- Exploring the Structures and Functions of Macromolecular SLX4-Nuclease Complexes in Genome Stability.Frontiers in genetics · 2021Review
- Article
- Resolution of the Holliday junction recombination intermediate by human GEN1 at the single-molecule level.Nucleic acids research · 2019Article
- Guidelines for DNA recombination and repair studies: Mechanistic assays of DNA repair processes.Microbial cell (Graz, Austria) · 2019Review
- Role of PCNA and RFC in promoting Mus81-complex activity.BMC biology · 2017Article
- The mismatch repair and meiotic recombination endonuclease Mlh1-Mlh3 is activated by polymer formation and can cleave DNA substrates in trans.PLoS biology · 2017Article
- The SMX DNA Repair Tri-nuclease.Molecular cell · 2017Article
- Review
- Meiotic Recombination: The Essence of Heredity.Cold Spring Harbor perspectives in biology · 2015Review
- The Slx4-Dpb11 scaffold complex: coordinating the response to replication fork stalling in S-phase and the subsequent mitosis.Cell cycle (Georgetown, Tex.) · 2015Article
- Review
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Authors and funding
4 authors.
Funding
Abstract
Mus81-Mms4/EME1 is a DNA structure-selective endonuclease that cleaves joint DNA molecules that form during homologous recombination in mitotic and meiotic cells. Here, we demonstrate by kinetic analysis using physically tethered DNA substrates that budding yeast Mus81-Mms4 requires inherent rotational flexibility in DNA junctions for optimal catalysis. Förster Resonance Energy Transfer experiments further reveal that recognition of 3'-flap and nicked Holliday junction substrates by Mus81-Mms4 involves induction of a sharp bend with a 100° angle between two duplex DNA arms. In addition, thiol crosslinking of Mus81-Mms4 bound to DNA junctions demonstrates that the heterodimer undergoes a conformational change induced by joint DNA molecules with preferred structural properties. The results from all three approaches suggest a model for catalysis by Mus81-Mms4 in which initial DNA binding is based on minimal structural requirements followed by a rate-limiting conformational transition of the substrate and protein. This leads to a sharply kinked DNA molecule that may fray the DNA four base pairs away from the junction point to position the nuclease for cleavage between the fourth and fifth nucleotide. These data suggest that mutually compatible conformational changes of Mus81-Mms4 and its substrates tailor its incision activity to nicked junction molecules.
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