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Literature summary for 2.7.7.7 extracted from

  • Zahurancik, W.J.; Suo, Z.
    Kinetic investigation of the polymerase and exonuclease activities of human DNA polymerase epsilon holoenzyme (2020), J. Biol. Chem., 295, 17251-17264 .
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D275A/E277A/D368A mutation in the catalytic subunit, exonuclease-deficient variant Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q07864 AND Q9NR33 AND P56282 AND Q9NRF9 Q07864: catalytic subunit A, Q9NR33: subunit 4, P56282: subunit 2, Q9NRF9: subunit 3
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Subunits

Subunits Comment Organism
heterotetramer the human DNA polymerase epsilon holoenzyme is comprised of the catalytic p261 subunit and the noncatalytic p59, p17, and p12 small subunits. The presence of the p261 C-terminal domain (p261C) and the three small subunits increased the DNA binding affinity and the base substitution fidelity Homo sapiens

Synonyms

Synonyms Comment Organism
DNA polymerase epsilon
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Homo sapiens
Polepsilon
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Homo sapiens

General Information

General Information Comment Organism
physiological function DNA polymerase epsilon (Pole) is responsible for leading strand synthesis. The presence of the C-terminal domain of the catalytic subunit (p261C) and the three small subunits regulates the 3'->5' exonuclease activity of the hPole holoenzyme. Together, the 3'->5 exonuclease activity and the variable mismatch extension activity modulate the overall fidelity of the hPole holoenzyme by up to 3 orders of magnitude. The presence of p261C and the three noncatalytic subunits optimizes the dual enzymatic activities of the catalytic p261 subunit and makes the hPole holoenzyme an efficient and faithful replicative DNA polymerase Homo sapiens