ArticleNucleic acids research1997
A structure-specific endonuclease from cauliflower (Brassica oleracea var. botrytis) inflorescence.
Article in Nucleic acids research, 1997. 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, 25 citations in OpenAlex.
- Plant tolerance mechanisms to DNA-damaging UV stress.Journal of experimental botany · 2025Review
- Base Excision DNA Repair in Plants:International journal of molecular sciences · 2023Review
- Structural Aspects of DNA Repair and Recombination in Crop Improvement.Frontiers in genetics · 2020Review
- DNA Base Excision Repair in Plants: An Unfolding Story With Familiar and Novel Characters.Frontiers in plant science · 2019Review
- Flap endonuclease 1.Annual review of biochemistry · 2013Review
- Regulating DNA replication in plants.Cold Spring Harbor perspectives in biology · 2012Review
- Rice exonuclease-1 homologue, OsEXO1, that interacts with DNA polymerase lambda and RPA subunit proteins, is involved in cell proliferation.Plant molecular biology · 2008Article
- DmGEN, a novel RAD2 family endo-exonuclease from Drosophila melanogaster.Nucleic acids research · 2004Article
- OsSEND-1: a new RAD2 nuclease family member in higher plants.Plant molecular biology · 2003Article
- A novel DNA polymerase homologous to Escherichia coli DNA polymerase I from a higher plant, rice (Oryza sativa L.).Nucleic acids research · 2002Article
- Plant homologue of flap endonuclease-1: molecular cloning, characterization, and evidence of expression in meristematic tissues.Plant molecular biology · 2000Article
- Characterization of Schizosaccharomyces pombe Rad2 protein, a FEN-1 homolog.Nucleic acids research · 1998Article
- Purification and characterization of a 100 kDa DNA polymerase from cauliflower inflorescence.The Biochemical journal · 1998Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A protein with structure-specific endonuclease activity has been purified to near homogeneity from cauliflower ( Brassica oleracea var. botrytis) inflorescence through five successive column chromatographies. The protein is a single polypeptide with a molecular mass of 40 kDa. Using three different branched DNA structures (flap, pseudo-Y and stem-loop) we found that the enzyme, a cauliflower structure-specific endonuclease, cleaved the single-stranded tail in the 5'-flap and 5'-pseudo-Y structures, whereas it could not incise the 3'-flap and 3'-pseudo-Y structures. The incision points occur around the single strand-duplex junction in these DNA substrates and the enzyme leaves 5'-PO4 and 3'-OH termini on DNA. The protein also endonucleolytically cleaves on the 3'-side of the single-stranded region at the junction of unpaired and duplex DNA in the stem-loop structure. The structure-specific endonuclease activity is stimulated by Mg2+ and by Mn2+, but not by Ca2+. Like mammalian FEN-1, the protein has weak 5'-->3' double-stranded DNA-specific exonuclease activity. These results indicate that the cauliflower protein is a plant structure-specific endonuclease like mammalian FEN-1 or may be the plant alternative.
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