NurA, a novel 5'-3' nuclease gene linked to rad50 and mre11 homologs of thermophilic Archaea.
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.
Constantinesco
Florence
F
Institut de Génétique et Microbiologie, UMR CNRS no 8621, Bâtiment 409, Université Paris-Sud, 91405 Orsay cedex, France.
Forterre
Patrick
P
Elie
Christiane
C
D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000235:genetics; D001426:Bacterial Proteins / Q000235:genetics; D004706:Endodeoxyribonucleases / Q000235:genetics; D005090:Exodeoxyribonucleases / Q000235:genetics*; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D016945:Sulfolobus acidocaldarius / Q000201:enzymology* / Q000235:genetics
D019843:Archaeal Proteins; D001426:Bacterial Proteins; D004706:Endodeoxyribonucleases; D005090:Exodeoxyribonucleases; C415985:Mre11 protein, archaeal; C415984:Rad50 protein, archaeal