TY - JOUR
T1 - PrimPol Variant V102A with Altered Primase and Polymerase Activities
AU - Boldinova, Elizaveta O.
AU - Baranovskiy, Andrey G.
AU - Filina, Yulia V.
AU - Miftakhova, Regina R.
AU - Shamsutdinova, Yana F.
AU - Tahirov, Tahir H.
AU - Makarova, Alena V.
N1 - Publisher Copyright:
© 2024 Elsevier Ltd
PY - 2024/5/1
Y1 - 2024/5/1
N2 - PrimPol is a human DNA primase-polymerase which restarts DNA synthesis beyond DNA lesions and non-B DNA structures blocking replication. Disfunction of PrimPol in cells leads to slowing of DNA replication rates in mitochondria and nucleus, accumulation of chromosome aberrations, cell cycle delay, and elevated sensitivity to DNA-damaging agents. A defective PrimPol has been suggested to be associated with the development of ophthalmic diseases, elevated mitochondrial toxicity of antiviral drugs and increased cell resistance to chemotherapy. Here, we describe a rare missense PrimPol variant V102A with altered biochemical properties identified in patients suffering from ovarian and cervical cancer. The Val102 to Ala substitution dramatically reduced both the primase and DNA polymerase activities of PrimPol as well as specifically decreased its ability to incorporate ribonucleotides. Structural analysis indicates that the V102A substitution can destabilize the hydrophobic pocket adjacent to the active site, affecting dNTP binding and catalysis.
AB - PrimPol is a human DNA primase-polymerase which restarts DNA synthesis beyond DNA lesions and non-B DNA structures blocking replication. Disfunction of PrimPol in cells leads to slowing of DNA replication rates in mitochondria and nucleus, accumulation of chromosome aberrations, cell cycle delay, and elevated sensitivity to DNA-damaging agents. A defective PrimPol has been suggested to be associated with the development of ophthalmic diseases, elevated mitochondrial toxicity of antiviral drugs and increased cell resistance to chemotherapy. Here, we describe a rare missense PrimPol variant V102A with altered biochemical properties identified in patients suffering from ovarian and cervical cancer. The Val102 to Ala substitution dramatically reduced both the primase and DNA polymerase activities of PrimPol as well as specifically decreased its ability to incorporate ribonucleotides. Structural analysis indicates that the V102A substitution can destabilize the hydrophobic pocket adjacent to the active site, affecting dNTP binding and catalysis.
KW - DNA translesion synthesis
KW - PrimPol
KW - active site
KW - single nucleotide polymorphism
KW - structure
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U2 - 10.1016/j.jmb.2024.168542
DO - 10.1016/j.jmb.2024.168542
M3 - Article
C2 - 38492718
AN - SCOPUS:85188520372
SN - 0022-2836
VL - 436
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 9
M1 - 168542
ER -