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Literature summary for 2.7.7.102 extracted from

  • Baranovskiy, A.; Zhang, Y.; Suwa, Y.; Gu, J.; Babayeva, N.; Pavlov, Y.; Tahirov, T.
    Insight into the human DNA primase interaction with template-primer (2016), J. Biol. Chem., 291, 4793-4802 .
    View publication on PubMedView publication on EuropePMC
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Activating Compound

Activating Compound Comment Organism Structure
KCl in the presence of Mg2+, primase activity is inhibited almost 4fold by increasing the KCl concentration from 15 mM to 150 mM. In the presence of Mn2+, KCl stimulates RNA synthesis Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
KCl in the presence of Mg2+, primase activity is inhibited almost 4fold by increasing the KCl concentration from 15 mM to 150 mM. In the presence of Mn2+, KCl stimulates RNA synthesis Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P49642 and P49643 P49642 i.e. small subunit Prim1, P49643 i.e. large subunit Prim2
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General Information

General Information Comment Organism
physiological function the C-terminal domain of the large subunit Prim2 plays a major role in template-primer binding and also defines the elements of the DNA template and the RNA primer that interact with the domain. The interaction with a template-primer involving the terminal 5'-triphosphate of RNA and the 3'-overhang of DNA results in a stable complex between the C-terminal domain of Prim2 and the DNA/RNA duplex Homo sapiens