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Literature summary for 5.6.2.4 extracted from
- The Sulfolobus solfataricus RecQ-like DNA helicase Hel112 inhibits the NurA/HerA complex exonuclease activity (2018), Extremophiles, 22, 581-589 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of His-tagged Hel112 in Escherichia coli strain Rosetta | Saccharolobus solfataricus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| DNA topoisomerase SsTop3 | inhibits the Hel112 helicase activity on Holliday junctions and stimulates formation and stabilization of such structures | Saccharolobus solfataricus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Saccharolobus solfataricus |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | Saccharolobus solfataricus | - |
ADP + phosphate | - |
? | |
| 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 | ? | - |
- |
|
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharolobus solfataricus | - |
i.e. Sulfolobus solfataricus | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| 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)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | - |
Saccharolobus solfataricus | ADP + phosphate | - |
? | |
| 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 | ? | - |
- |
|
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Hel112 | - |
Saccharolobus solfataricus |
| RecQ-like DNA helicase | - |
Saccharolobus solfataricus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
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