ArticleNucleic acids research2004
DmGEN, a novel RAD2 family endo-exonuclease from Drosophila melanogaster.
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 13 papers.
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Who cites it
13 citing papers in PubMed, 21 citations in OpenAlex.
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- Canonical and novel non-canonical activities of the Holliday junction resolvase Yen1.Nucleic acids research · 2022Article
- Specific Human ATR and ATM Inhibitors Modulate Single Strand DNA Formation inFrontiers in cellular and infection microbiology · 2021Article
- Review
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- Human Holliday junction resolvase GEN1 uses a chromodomain for efficient DNA recognition and cleavage.eLife · 2015Article
- Meiotic Recombination: The Essence of Heredity.Cold Spring Harbor perspectives in biology · 2015Review
- Holliday junction resolvases.Cold Spring Harbor perspectives in biology · 2014Review
- Genetic analysis of mlh3 mutations reveals interactions between crossover promoting factors during meiosis in baker's yeast.G3 (Bethesda, Md.) · 2013Article
- Article
- Three structure-selective endonucleases are essential in the absence of BLM helicase in Drosophila.PLoS genetics · 2011Article
- Processing of joint molecule intermediates by structure-selective endonucleases during homologous recombination in eukaryotes.Chromosoma · 2011Review
- Rice exonuclease-1 homologue, OsEXO1, that interacts with DNA polymerase lambda and RPA subunit proteins, is involved in cell proliferation.Plant molecular biology · 2008Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A novel endo-exonuclease, DmGEN (Drosophila Melanogaster XPG-like endonuclease), was identified in D.melanogaster. DmGEN is composed of five exons and four introns, and the open reading frame encodes a predicted product of 726 amino acid residues with a molecular weight of 82.5 kDa and a pI of 5.36. The gene locus on Drosophila polytene chromosomes was detected at 64C9 on the left arm of chromosome 3 as a single site. The encoded protein showed a relatively high degree of sequence homology with the RAD2 nucleases, especially XPG. Although the XPG-N- and XPG-I-domains are highly conserved in sequence, locations of the domains are similar to those of FEN-1 and EXO-1, and the molecular weight of the protein is close to that of EXO-1. In vitro, DmGEN showed endonuclease and 3'-5' exonuclease activities with both single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA), but the endonuclease action with dsDNA was quite specific: 5'-3' exonuclease activity was found to occur with nicked DNA, while dsDNA was endonucleolytically cut at 3-4 bp from the 5' end. Homologs are widely found in mammals and higher plants. The data suggest that DmGEN belongs to a new class of RAD2 nuclease.
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