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- W4225392322 abstract "ABSTRACT The human primosome, a four-subunit complex of primase and DNA polymerase alpha (Polα), synthesizes chimeric RNA-DNA primers for DNA polymerases delta and epsilon to initiate DNA replication on both chromosome strands. Despite recent structural insights into the action of its two catalytic centers, the mechanism of DNA synthesis termination is still unclear. Here we report results of functional and structural studies revealing how the human primosome counts RNA-DNA primer length and timely terminates DNA elongation. Using a single-turnover primer extension assay, we defined two factors that determine a mature primer length (~35-mer): 1) a tight interaction of the C-terminal domain of the DNA primase large subunit (p58 C ) with the primer 5’-end, and 2) flexible tethering of p58 C and the DNA polymerase alpha catalytic core domain (p180 core ) to the primosome platform domain by extended linkers. The obtained data allows us to conclude that p58 C is a key regulator of all steps of RNA-DNA primer synthesis. The above-described findings provide a notable insight into the mechanism of DNA synthesis termination by a eukaryotic primosome, an important process for ensuring successful primer handover to replication DNA polymerases and for maintaining genome integrity." @default.
- W4225392322 created "2022-05-05" @default.
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- W4225392322 date "2022-05-02" @default.
- W4225392322 modified "2023-09-26" @default.
- W4225392322 title "Insight into RNA-DNA primer length counting by human primosome" @default.
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- W4225392322 doi "https://doi.org/10.1101/2022.05.02.490354" @default.
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