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Tytuł pozycji:

DNA polymerase D temporarily connects primase to the CMG-like helicase before interacting with proliferating cell nuclear antigen.

Tytuł:
DNA polymerase D temporarily connects primase to the CMG-like helicase before interacting with proliferating cell nuclear antigen.
Autorzy:
Oki K; Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, Fukuoka, Japan.
Yamagami T; Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, Fukuoka, Japan.
Nagata M; Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, Fukuoka, Japan.
Mayanagi K; Medical Institute of Bioregulation, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka-shi, Fukuoka 812-8582, Japan.
Shirai T; Department of Bioscience, Nagahama Institute of Bio-Science and Technology, Tamura 1266, Nagahama, Shiga 526-0829, Japan.
Adachi N; Structure Biology Research Center, Institute of Materials Structural Science, High Energy Accelerator Research Organization, 1-1 Oho, Tsukuba, Ibaraki 305-0801, Japan.
Numata T; Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, Fukuoka, Japan.
Ishino S; Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, Fukuoka, Japan.
Ishino Y; Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, Fukuoka, Japan.
Źródło:
Nucleic acids research [Nucleic Acids Res] 2021 May 07; Vol. 49 (8), pp. 4599-4612.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
Język:
English
Imprint Name(s):
Publication: 1992- : Oxford : Oxford University Press
Original Publication: London, Information Retrieval ltd.
MeSH Terms:
Archaeal Proteins/*metabolism
DNA Helicases/*metabolism
DNA Polymerase III/*metabolism
DNA Primase/*chemistry
Proliferating Cell Nuclear Antigen/*metabolism
Thermococcus/*metabolism
Amino Acid Motifs ; Archaeal Proteins/chemistry ; Chromatography, Gel ; DNA Helicases/genetics ; DNA Polymerase III/chemistry ; DNA Primase/genetics ; DNA Primase/metabolism ; Escherichia coli/metabolism ; Hydrophobic and Hydrophilic Interactions ; Mutagenesis, Site-Directed ; Native Polyacrylamide Gel Electrophoresis ; Proliferating Cell Nuclear Antigen/genetics ; Protein Binding ; Recombinant Proteins ; Surface Plasmon Resonance ; Thermococcus/genetics
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Substance Nomenclature:
0 (Archaeal Proteins)
0 (Proliferating Cell Nuclear Antigen)
0 (Recombinant Proteins)
EC 2.7.7.- (DNA Primase)
EC 2.7.7.7 (DNA Polymerase III)
EC 3.6.4.- (DNA Helicases)
Entry Date(s):
Date Created: 20210413 Date Completed: 20210616 Latest Revision: 20210616
Update Code:
20240104
PubMed Central ID:
PMC8096248
DOI:
10.1093/nar/gkab243
PMID:
33849056
Czasopismo naukowe
The eukaryotic replisome is comprised of three family-B DNA polymerases (Polα, δ and ϵ). Polα forms a stable complex with primase to synthesize short RNA-DNA primers, which are subsequently elongated by Polδ and Polϵ in concert with proliferating cell nuclear antigen (PCNA). In some species of archaea, family-D DNA polymerase (PolD) is the only DNA polymerase essential for cell viability, raising the question of how it alone conducts the bulk of DNA synthesis. We used a hyperthermophilic archaeon, Thermococcus kodakarensis, to demonstrate that PolD connects primase to the archaeal replisome before interacting with PCNA. Whereas PolD stably connects primase to GINS, a component of CMG helicase, cryo-EM analysis indicated a highly flexible PolD-primase complex. A conserved hydrophobic motif at the C-terminus of the DP2 subunit of PolD, a PIP (PCNA-Interacting Peptide) motif, was critical for the interaction with primase. The dissociation of primase was induced by DNA-dependent binding of PCNA to PolD. Point mutations in the alternative PIP-motif of DP2 abrogated the molecular switching that converts the archaeal replicase from de novo to processive synthesis mode.
(© The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research.)

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