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- W4226177540 abstract "Abstract Homologous recombination-deficient cancers rely on DNA polymerase Theta (Polθ)-Mediated End Joining (TMEJ), an alternative double-strand break repair pathway. Polθ is the only vertebrate polymerase that encodes an N-terminal superfamily 2 (SF2) helicase domain, but the role of this helicase domain in TMEJ remains unclear. Using single-molecule imaging, we demonstrate that Polθ-helicase (Polθ-h) is a highly processive single-stranded DNA (ssDNA) motor protein that can efficiently strip Replication Protein A (RPA) from ssDNA. Polθ-h also has a limited capacity for disassembling RAD51 filaments but is not processive on double-stranded DNA. Polθ-h can bridge two non-complementary DNA strands in trans. PARylation of Polθ-h by PARP-1 resolves these DNA bridges. We conclude that Polθ-h removes RPA and RAD51 filaments and mediates bridging of DNA overhangs to aid in polymerization by the Polθ polymerase domain." @default.
- W4226177540 created "2022-05-05" @default.
- W4226177540 creator A5006271100 @default.
- W4226177540 creator A5035025102 @default.
- W4226177540 creator A5049172093 @default.
- W4226177540 date "2022-03-31" @default.
- W4226177540 modified "2023-09-30" @default.
- W4226177540 title "Polymerase theta-helicase promotes end joining by stripping single-stranded DNA-binding proteins and bridging DNA ends" @default.
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- W4226177540 doi "https://doi.org/10.1093/nar/gkac119" @default.
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