ArticleCell reports2020
Dynamic Assembly and Disassembly of the Human DNA Polymerase δ Holoenzyme on the Genome In Vivo.
Article in Cell reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 28 citations in OpenAlex.
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- Prospects of POLD1 in Human Cancers: A Review.Cancers · 2023Review
- Mechanistic investigation of human maturation of Okazaki fragments reveals slow kinetics.Nature communications · 2022Article
- Bromodomains regulate dynamic targeting of the PBAF chromatin-remodeling complex to chromatin hubs.Biophysical journal · 2022Article
- POLD2 is activated by E2F1 to promote triple-negative breast cancer proliferation.Frontiers in oncology · 2022Article
- Locus-Specific Analysis of Replication Dynamics and Detection of DNA-RNA Hybrids by Immuno Electron Microscopy.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Micro-Meta App: an interactive tool for collecting microscopy metadata based on community specifications.Nature methods · 2021Article
- TERRA G-quadruplex RNA interaction with TRF2 GAR domain is required for telomere integrity.Scientific reports · 2021Article
- TRF2 Mediates Replication Initiation within Human Telomeres to Prevent Telomere Dysfunction.Cell reports · 2020Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Human DNA polymerase delta (Pol δ) forms a holoenzyme complex with the DNA sliding clamp proliferating cell nuclear antigen (PCNA) to perform its essential roles in genome replication. Here, we utilize live-cell single-molecule tracking to monitor Pol δ holoenzyme interaction with the genome in real time. We find holoenzyme assembly and disassembly in vivo are highly dynamic and ordered. PCNA generally loads onto the genome before Pol δ. Once assembled, the holoenzyme has a relatively short lifetime on the genome, implying multiple Pol δ binding events may be needed to synthesize an Okazaki fragment. During disassembly, Pol δ dissociation generally precedes PCNA unloading. We also find that Pol δ p125, the catalytic subunit of the holoenzyme, is maintained at a constant cellular level, indicating an active mechanism for control of Pol δ levels in vivo. Collectively, our studies reveal that Pol δ holoenzyme assembly and disassembly follow a predominant pathway in vivo; however, alternate pathways are observed.
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