ArticleeLife2015
Human Holliday junction resolvase GEN1 uses a chromodomain for efficient DNA recognition and cleavage.
Article in eLife, 2015. 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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Who cites it
26 citing papers in PubMed, 36 citations in OpenAlex.
- Pathogenic variants in MAEA disrupt DNA replication fork stability and are associated with developmental abnormalities in humans.Science advances · 2025Article
- Targeted and Untargeted Proteomics-based Comparison of Adenoviral Infected hCMEC/D3 and hBMEC as a Human Brain Endothelial Cells to Study the OATP2B1 Transporter.Molecular neurobiology · 2025Article
- MOC1 cleaves Holliday junctions through a cooperative nick and counter-nick mechanism mediated by metal ions.Nature communications · 2024Article
- Genomic alterations in ovarian endometriosis and subsequently diagnosed ovarian carcinoma.Human reproduction (Oxford, England) · 2024Article
- GEN1 as a risk factor for human congenital anomalies of the kidney and urinary tract.Human genomics · 2024Article
- Structural Motifs at the Telomeres and Their Role in Regulatory Pathways.Biochemistry · 2024Review
- Reverse Transcription-PCR-based Sanger Sequencing-confirmed Exon-skipping Effect of a NovelAnnals of laboratory medicine · 2024Article
- DNA Holliday Junction: History, Regulation and Bioactivity.International journal of molecular sciences · 2022Review
- Canonical and novel non-canonical activities of the Holliday junction resolvase Yen1.Nucleic acids research · 2022Article
- Implementing fluorescence enhancement, quenching, and FRET for investigating flap endonuclease 1 enzymatic reaction at the single-molecule level.Computational and structural biotechnology journal · 2021Review
- The crystal structure of human XPG, the xeroderma pigmentosum group G endonuclease, provides insight into nucleotide excision DNA repair.Nucleic acids research · 2020Article
- Human XPG nuclease structure, assembly, and activities with insights for neurodegeneration and cancer from pathogenic mutations.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Structural insights into sequence-dependent Holliday junction resolution by the chloroplast resolvase MOC1.Nature communications · 2020Article
- Structural Aspects of DNA Repair and Recombination in Crop Improvement.Frontiers in genetics · 2020Review
- Recognition and processing of branched DNA substrates by Slx1-Slx4 nuclease.Nucleic acids research · 2019Article
- Review
- Resolution of the Holliday junction recombination intermediate by human GEN1 at the single-molecule level.Nucleic acids research · 2019Article
- A monovalent ion in the DNA binding interface of the eukaryotic junction-resolving enzyme GEN1.Nucleic acids research · 2018Article
- Regional conformational flexibility couples substrate specificity and scissile phosphate diester selectivity in human flap endonuclease 1.Nucleic acids research · 2018Article
- Crystal structure and mutational analysis of Mycobacterium smegmatis FenA highlight active site amino acids and three metal ions essential for flap endonuclease and 5' exonuclease activities.Nucleic acids research · 2018Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Holliday junctions (HJs) are key DNA intermediates in homologous recombination. They link homologous DNA strands and have to be faithfully removed for proper DNA segregation and genome integrity. Here, we present the crystal structure of human HJ resolvase GEN1 complexed with DNA at 3.0 Å resolution. The GEN1 core is similar to other Rad2/XPG nucleases. However, unlike other members of the superfamily, GEN1 contains a chromodomain as an additional DNA interaction site. Chromodomains are known for their chromatin-targeting function in chromatin remodelers and histone(de)acetylases but they have not previously been found in nucleases. The GEN1 chromodomain directly contacts DNA and its truncation severely hampers GEN1's catalytic activity. Structure-guided mutations in vitro and in vivo in yeast validated our mechanistic findings. Our study provides the missing structure in the Rad2/XPG family and insights how a well-conserved nuclease core acquires versatility in recognizing diverse substrates for DNA repair and maintenance.
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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.