title: Characteristic thermodependence of the RadA recombinase from the hyperthermophilic archaeon Desulfurococcus amylolyticus.
abstract: The Desulfurococcus amylolyticus RadA protein (RadA(Da)) promotes recombination at temperatures approaching the DNA melting point. Here, analyzing ATPase of the RadA(Da) presynaptic complex, we described other distinguishing characteristics of RadA(Da). These include sensitivity to NaCl, preference for lengthy single-stranded DNA as a cofactor, protein activity at temperatures of over 100 degrees C, and bimodal ATPase activity. These characteristics suggest that RadA(Da) is a founding member of a new class of archaeal recombinases.
authors.affiliation: Division of Molecular and Radiation Biophysics, Petersburg Nuclear Physics Institute, Russian Academy of Sciences, Gatchina/St. Petersburg 188300, Russia.
authors.forename: Yury V
authors.initials: YV
authors.lastname: Kil
authors.forename: Eugene A
authors.initials: EA
authors.lastname: Glazunov
authors.forename: Vladislav A
authors.initials: VA
authors.lastname: Lanzov
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D019843:Archaeal Proteins / Q000737:chemistry / Q000378:metabolism*; D019641:DNA, Archaeal / Q000737:chemistry / Q000378:metabolism; D004277:DNA, Single-Stranded / Q000737:chemistry / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D019620:Desulfurococcaceae / Q000187:drug effects / Q000201:enzymology*; D004795:Enzyme Stability; D006358:Hot Temperature; D045522:Recombinases / Q000737:chemistry / Q000378:metabolism*; D012965:Sodium Chloride / Q000494:pharmacology; D013816:Thermodynamics
chemical_list: D019843:Archaeal Proteins; D019641:DNA, Archaeal; D004277:DNA, Single-Stranded; D004268:DNA-Binding Proteins; C117252:RadA protein, archaeal; D045522:Recombinases; D012965:Sodium Chloride; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases