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Literature summary for 5.6.2.4 extracted from

  • Blackwood, J.K.; Rzechorzek, N.J.; Abrams, A.S.; Maman, J.D.; Pellegrini, L.; Robinson, N.P.
    Structural and functional insights into DNA-end processing by the archaeal HerA helicase-NurA nuclease complex (2012), Nucleic Acids Res., 40, 3183-3196.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.2.4

Activating Compound

Activating Compound Comment Organism Structure
additional information in isolation, HerA helicase and NurA nuclease possess little or no enzymatic activity. Efficient processing of DNA ends requires their reconstitution in a specific physical complex Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus
-
-
-
Saccharolobus solfataricus P2
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharolobus solfataricus

Subunits

Subunits Comment Organism
More in isolation, HerA helicase and NurA nuclease possess little or no enzymatic activity. Efficient processing of DNA ends requires their reconstitution in a specific physical complex. The complex is composed of a HerA hexamer bound to a NurA dimer Saccharolobus solfataricus

Synonyms

Synonyms Comment Organism
HerA helicase
-
 Saccharolobus solfataricus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30 95 no unfolding in the temperature range 30–95°C, indicating that its Tm is greater than 95°C Saccharolobus solfataricus

General Information

General Information Comment Organism
physiological function in thermophilic archaea, the HerA helicase and NurA nuclease cooperate with the highly conserved Mre11 and Rad50 proteins during homologous recombination-dependent DNA repair Saccharolobus solfataricus