ArticleProceedings of the National Academy of Sciences of the United States of America2017
Resolution of single and double Holliday junction recombination intermediates by GEN1.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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26 citing papers in PubMed, 46 citations in OpenAlex.
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- DNA Holliday Junction: History, Regulation and Bioactivity.International journal of molecular sciences · 2022Review
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- Generation of double Holliday junction DNAs and their dissolution/resolution within a chromatin context.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Canonical and novel non-canonical activities of the Holliday junction resolvase Yen1.Nucleic acids research · 2022Article
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- Meiotic Recombination Defects and Premature Ovarian Insufficiency.Frontiers in cell and developmental biology · 2021Review
- Structural insights into sequence-dependent Holliday junction resolution by the chloroplast resolvase MOC1.Nature communications · 2020Article
- The Therapeutic Potential of DNA Damage Repair Pathways and Genomic Stability in Lung Cancer.Frontiers in oncology · 2020Review
- DNA Damage Response and Oxidative Stress in Systemic Autoimmunity.International journal of molecular sciences · 2019Review
- Review
- Resolution of the Holliday junction recombination intermediate by human GEN1 at the single-molecule level.Nucleic acids research · 2019Article
- Rescue of collapsed replication forks is dependent on NSMCE2 to prevent mitotic DNA damage.PLoS genetics · 2019Article
- Spatiotemporal dynamics of homologous recombination repair at single collapsed replication forks.Nature communications · 2018Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Genetic recombination provides an important mechanism for the repair of DNA double-strand breaks. Homologous pairing and strand exchange lead to the formation of DNA intermediates, in which sister chromatids or homologous chromosomes are covalently linked by four-way Holliday junctions (HJs). Depending on the type of recombination reaction that takes place, intermediates may have single or double HJs, and their resolution is essential for proper chromosome segregation. In mitotic cells, double HJs are primarily dissolved by the BLM helicase-TopoisomeraseIIIα-RMI1-RMI2 (BTR) complex, whereas single HJs (and double HJs that have escaped the attention of BTR) are resolved by structure-selective endonucleases known as HJ resolvases. These enzymes are ubiquitous in nature, because they are present in bacteriophage, bacteria, archaea, and simple and complex eukaryotes. The human HJ resolvase GEN1 is a member of the XPG/Rad2 family of 5'-flap endonucleases. Biochemical studies of GEN1 revealed that it cleaves synthetic DNA substrates containing a single HJ by a mechanism similar to that shown by the prototypic HJ resolvase, Escherichia coli RuvC protein, but it is unclear whether these substrates fully recapitulate the properties of recombination intermediates that arise within a physiological context. Here, we show that GEN1 efficiently cleaves both single and double HJs contained within large recombination intermediates. Moreover, we find that GEN1 exhibits a weak sequence preference for incision between two G residues that reside in a T-rich region of DNA. These results contrast with those obtained with RuvC, which exhibits a strict requirement for the consensus sequence 5'-
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