ArticleProceedings of the National Academy of Sciences of the United States of America2008
Cleavage mechanism of human Mus81-Eme1 acting on Holliday-junction structures.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 67 citations in OpenAlex.
- Combined strategies with PARP inhibitors for the treatment of BRCA wide type cancer.Frontiers in oncology · 2024Review
- Pharmacologic Induction of BRCAness inCancers · 2022Review
- Regulation of Mus81-Eme1 structure-specific endonuclease by Eme1 SUMO-binding and Rad3ATR kinase is essential in the absence of Rqh1BLM helicase.PLoS genetics · 2022Article
- EXO5-DNA structure and BLM interactions direct DNA resection critical for ATR-dependent replication restart.Molecular cell · 2021Article
- Tobacco Smoke Carcinogens Induce DNA Repair Machinery Function Loss: Protection by Carbon Nanotubes.Asian Pacific journal of cancer prevention : APJCP · 2020Article
- Article
- Resolvase OsGEN1 Mediates DNA Repair by Homologous Recombination.Plant physiology · 2017Article
- Cooperation of Blm and Mus81 in development, fertility, genomic integrity and cancer suppression.Oncogene · 2015Article
- Quality control of homologous recombination.Cellular and molecular life sciences : CMLS · 2014Review
- Holliday junction resolvases.Cold Spring Harbor perspectives in biology · 2014Review
- Human MUS81-EME2 can cleave a variety of DNA structures including intact Holliday junction and nicked duplex.Nucleic acids research · 2014Article
- Substrate specificity of the MUS81-EME2 structure selective endonuclease.Nucleic acids research · 2014Article
- A winged helix domain in human MUS81 binds DNA and modulates the endonuclease activity of MUS81 complexes.Nucleic acids research · 2013Article
- Cooperative control of holliday junction resolution and DNA repair by the SLX1 and MUS81-EME1 nucleases.Molecular cell · 2013Article
- Human GEN1 and the SLX4-associated nucleases MUS81 and SLX1 are essential for the resolution of replication-induced Holliday junctions.Cell reports · 2013Article
- Survival of the replication checkpoint deficient cells requires MUS81-RAD52 function.PLoS genetics · 2013Article
- Temporal regulation of the Mus81-Mms4 endonuclease ensures cell survival under conditions of DNA damage.Nucleic acids research · 2013Article
- Effect of EME1 exon variant Ile350Thr on risk and early onset of breast cancer in southern Chinese women.Journal of biomedical research · 2013Article
- Oncogenes induce genotoxic stress by mitotic processing of unusual replication intermediates.The Journal of cell biology · 2013Article
- Holliday junction affinity of the base excision repair factor Endo III contributes to cholera toxin phage integration.The EMBO journal · 2012Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recombination-mediated repair plays a central role in maintaining genomic integrity during DNA replication. The human Mus81-Eme1 endonuclease is involved in recombination repair, but the exact structures it acts on in vivo are not known. Using kinetic and enzymatic analysis of highly purified recombinant enzyme, we find that Mus81-Eme1 catalyzes coordinate bilateral cleavage of model Holliday-junction structures. Using a self-limiting, cruciform-containing substrate, we demonstrate that bilateral cleavage occurs sequentially within the lifetime of the enzyme-substrate complex. Coordinate bilateral cleavage is promoted by the highly cooperative nature of the enzyme and results in symmetrical cleavage of a cruciform structure, thus, Mus81-Eme1 can ensure coordinate, bilateral cleavage of Holliday junction-like structures.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.