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TitleHuman primosome requires replication protein A when copying DNA with inverted repeats.
Journal, issue, pagesbioRxiv, Year 2025
Publish dateJan 28, 2025
AuthorsAndrey Baranovskiy / Lucia Morstadt / Eduardo E Romero / Nigar Babayeva / Tahir H Tahirov
PubMed AbstractThe human primosome, a four-subunit complex of primase and DNA polymerase alpha (Polα), initiates DNA synthesis on both chromosome strands by generating chimeric RNA-DNA primers for loading DNA ...The human primosome, a four-subunit complex of primase and DNA polymerase alpha (Polα), initiates DNA synthesis on both chromosome strands by generating chimeric RNA-DNA primers for loading DNA polymerases delta and epsilon (Polε). Replication protein A (RPA) tightly binds to single-stranded DNA strands, protecting them from nucleolytic digestion and unauthorized transactions. We report here that RPA plays a critical role for the human primosome during DNA synthesis across inverted repeats prone to hairpin formation. On other alternatively structured DNA, forming a G-quadruplex, RPA does not assist primosome. A stimulatory effect of RPA on DNA synthesis across hairpins was also observed for the catalytic domain of Polα but not of Polε. The winged helix-turn-helix domain of RPA is essential for an efficient hairpin bypass and increases RPA-Polα cooperativity on the primed DNA template. Cryo-EM studies revealed that this domain is mainly responsible for the interaction between RPA and Polα. The flexible mode of RPA-Polα interaction during DNA synthesis implies the mechanism of template handover between them when the hairpin formation should be avoided. This work provides insight into a cooperative action of RPA and primosome on DNA, which is critical for DNA synthesis across inverted repeats.
External linksbioRxiv / PubMed:38559116 / PubMed Central
MethodsEM (single particle)
Resolution3.49 - 4.21 Å
Structure data

EMDB-49101: Catalytic domain of human DNA polymerase alpha in complex with DNA and RPA (consensus map)
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-49102: Catalytic domain of human DNA polymerase alpha in complex with DNA and RPA (rpa focused map)
Method: EM (single particle) / Resolution: 4.21 Å

EMDB-49103: Catalytic domain of human DNA polymerase alpha in complex with DNA and RPA (focused map for PolA/DNA)
Method: EM (single particle) / Resolution: 3.49 Å

Source
  • Homo sapiens (human)

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