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Literature summary extracted from

  • De Falco, M.; Massa, F.; Rossi, M.; De Felice, M.
    The Sulfolobus solfataricus RecQ-like DNA helicase Hel112 inhibits the NurA/HerA complex exonuclease activity (2018), Extremophiles, 22, 581-589 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.6.2.4 recombinant expression of His-tagged Hel112 in Escherichia coli strain Rosetta Saccharolobus solfataricus

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.6.2.4 DNA topoisomerase SsTop3 inhibits the Hel112 helicase activity on Holliday junctions and stimulates formation and stabilization of such structures Saccharolobus solfataricus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.6.2.4 Mg2+ required Saccharolobus solfataricus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.6.2.4 ATP + H2O Saccharolobus solfataricus
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 ADP + phosphate
-
 ?
5.6.2.4 additional information Saccharolobus solfataricus Hel112 physically interacts with the Saccharolobus solfataricus DNA topoisomerase SsTop3, and the two enzymes show synergic and opposing activities. SsTop3 inhibits the Hel112 helicase activity on Holliday junctions and stimulates formation and stabilization of such structures ?
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Organism

EC Number Organism UniProt Comment Textmining
5.6.2.4 Saccharolobus solfataricus
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 i.e. Sulfolobus solfataricus
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Purification (Commentary)

EC Number Purification (Comment) Organism
5.6.2.4 recombinant His-tagged Hel112 from Escherichia coli strain Rosetta by heat treatment at 80°C for 20 min, nickel affinity chromatography, dialysis, heparin affinity chromatography, and ultrafiltration Saccharolobus solfataricus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.6.2.4 ATP + H2O
-
 Saccharolobus solfataricus ADP + phosphate
-
 ?
5.6.2.4 additional information Hel112 physically interacts with the Saccharolobus solfataricus DNA topoisomerase SsTop3, and the two enzymes show synergic and opposing activities. SsTop3 inhibits the Hel112 helicase activity on Holliday junctions and stimulates formation and stabilization of such structures Saccharolobus solfataricus ?
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-

Synonyms

EC Number Synonyms Comment Organism
5.6.2.4 Hel112
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 Saccharolobus solfataricus
5.6.2.4 RecQ-like DNA helicase
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 Saccharolobus solfataricus

General Information

EC Number General Information Comment Organism
5.6.2.4 evolution the enzyme belongs to the RecQ protein family, a group of helicases highly conserved from bacteria to humans and playing a critical role in transcription, DNA replication, DNA recombination, and DNA repair Saccharolobus solfataricus
5.6.2.4 physiological function in hyperthermophilic archaea the exo-endonuclease NurA and the ATPase HerA cooperate with the highly conserved Mre11-Rad50 complex in 3' single-stranded DNA (ssDNA) end processing to coordinate repair of double-stranded DNA breaks. RecQ-like DNA helicase Hel112 inhibits the NurA/HerA complex exonuclease activity on linear dsDNA and ssDNA substrates. This effect is not dependent on the directionality of the complex activity. Inhibition occurs both in the presence and in the absence of HerA, but is much stronger when NurA is in complex with HerA. The endonuclease activity of NurA is not affected by the presence of Hel112. The functional interaction between NurA/HerA and Hel112 is important for DNA endresection in archaeal homologous recombination. But Hel112 has no effect on NurA/HerA nicking activity, the inhibitory effect of Hel112 is specific for NurA/HerA exonuclease activity Saccharolobus solfataricus