WRNIP1 Controls the Amount of PrimPol
Autor: | Yuri Hasegawa, Takemi Enomoto, Mizuho Oikawa, Akari Yoshimura, Masayuki Seki, Hitomi Jinbo |
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Rok vydání: | 2019 |
Předmět: |
0301 basic medicine
DNA Complementary DNA polymerase Pharmaceutical Science DNA Primase DNA-Directed DNA Polymerase Transfection 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine WRNIP1 medicine Humans RNA Messenger Gene Polymerase Werner syndrome Pharmacology biology DNA synthesis Chemistry General Medicine medicine.disease Multifunctional Enzymes Cell biology DNA-Binding Proteins HEK293 Cells 030104 developmental biology Proteasome 030220 oncology & carcinogenesis biology.protein ATPases Associated with Diverse Cellular Activities Proteasome Inhibitors DNA Plasmids |
Zdroj: | Biological and Pharmaceutical Bulletin. 42:764-769 |
ISSN: | 1347-5215 0918-6158 |
DOI: | 10.1248/bpb.b18-00955 |
Popis: | Werner helicase-interacting protein 1 (WRNIP1) was originally identified as a protein that interacts with WRN, the product of the gene responsible for Werner syndrome. Our previous studies suggested that WRNIP1 is implicated in translesion synthesis (TLS), a process in which specialized TLS polymerases replace replicative DNA polymerase and take over DNA synthesis on damaged templates. We proposed that a novel error-free pathway involving DNA polymerase δ and primase-polymerase (PrimPol) functions to synthesize DNA on UV-damaged DNA templates in the absence of WRNIP1 and the TLS polymerase Polη. Hence, in the current study, we analyzed the relationship between WRNIP1 and PrimPol. We found that WRNIP1 and PrimPol form a complex in cells. PrimPol protein expression was reduced in cells overexpressing WRNIP1, but was increased in WRNIP1-depleted cells. The WRNIP1-mediated reduction in the amount of PrimPol was suppressed by treatment of the cells with proteasome inhibitors, suggesting that WRNIP1 is involved in the degradation of PrimPol via the proteasome. |
Databáze: | OpenAIRE |
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