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NurA , a novel 5′–3′ nuclease gene linked to rad50 and mre11 homologs of thermophilic Archaea
Author(s) -
Constantinesco Florence,
Forterre Patrick,
Elie Christiane
Publication year - 2002
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1093/embo-reports/kvf112
Subject(s) - nuclease , exonuclease , rad50 , thermophile , sulfolobus , homologous recombination , biology , sulfolobus acidocaldarius , genetics , operon , archaea , dna , gene , dna repair , recbcd , rad51 , biochemistry , dna binding protein , bacteria , dna polymerase , escherichia coli , transcription factor
We isolated and characterized a new nuclease (NurA) exhibiting both single‐stranded endonuclease activity and 5′–3′ exonuclease activity on single‐stranded and double‐stranded DNA from the hyperthermophilic archaeon Sulfolobus acidocaldarius . Nuclease homologs are detected in all thermophilic archaea and, in most species, the nurA gene is organized in an operon‐like structure with rad50 and mre11 archaeal homologs. This nuclease might thus act in concert with Rad50 and Mre11 proteins in archaeal recombination/repair. To our knowledge, this is the first report of a 5′–3′ nuclease potentially associated with Rad50 and Mre11‐like proteins that may lead to the processing of double‐stranded breaks in 3′ single‐stranded tails.