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古细菌复制体中DNA聚合酶与复制蛋白A之间的通讯

Communication between DNA polymerases and Replication Protein A within the archaeal replisome.

作者信息

Martínez-Carranza Markel, Vialle Léa, Madru Clément, Cordier Florence, Tekpinar Ayten Dizkirici, Haouz Ahmed, Legrand Pierre, Le Meur Rémy A, England Patrick, Dulermo Rémi, Guijarro J Iñaki, Henneke Ghislaine, Sauguet Ludovic

机构信息

Architecture and Dynamics of Biological Macromolecules, Institut Pasteur, Université Paris Cité, CNRS UMR 3528, Paris, France.

Univ Brest, Ifremer, CNRS, Biologie et Ecologie des Ecoystèmes marins profonds (BEEP), Plouzané, France.

出版信息

Nat Commun. 2024 Dec 30;15(1):10926. doi: 10.1038/s41467-024-55365-w.

DOI:10.1038/s41467-024-55365-w
PMID:39738083
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11686378/
Abstract

Replication Protein A (RPA) plays a pivotal role in DNA replication by coating and protecting exposed single-stranded DNA, and acting as a molecular hub that recruits additional replication factors. We demonstrate that archaeal RPA hosts a winged-helix domain (WH) that interacts with two key actors of the replisome: the DNA primase (PriSL) and the replicative DNA polymerase (PolD). Using an integrative structural biology approach, combining nuclear magnetic resonance, X-ray crystallography and cryo-electron microscopy, we unveil how RPA interacts with PriSL and PolD through two distinct surfaces of the WH domain: an evolutionarily conserved interface and a novel binding site. Finally, RPA is shown to stimulate the activity of PriSL in a WH-dependent manner. This study provides a molecular understanding of the WH-mediated regulatory activity in central replication factors such as RPA, which regulate genome maintenance in Archaea and Eukaryotes.

摘要

复制蛋白A（RPA）通过包裹和保护暴露的单链DNA，并作为招募其他复制因子的分子枢纽，在DNA复制中发挥关键作用。我们证明古细菌RPA拥有一个翼状螺旋结构域（WH），该结构域与复制体的两个关键因子相互作用：DNA引发酶（PriSL）和复制性DNA聚合酶（PolD）。通过结合核磁共振、X射线晶体学和冷冻电子显微镜的综合结构生物学方法，我们揭示了RPA如何通过WH结构域的两个不同表面与PriSL和PolD相互作用：一个进化上保守的界面和一个新的结合位点。最后，RPA被证明以WH依赖的方式刺激PriSL的活性。这项研究提供了对WH介导的在诸如RPA等中心复制因子中的调节活性的分子理解，RPA在古细菌和真核生物中调节基因组维持。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9da7/11686378/3b1a52374591/41467_2024_55365_Fig8_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9da7/11686378/8cb7b636b4a4/41467_2024_55365_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9da7/11686378/a2ba078bb5bc/41467_2024_55365_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9da7/11686378/3e59ec40cb23/41467_2024_55365_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9da7/11686378/3c51e96ea940/41467_2024_55365_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9da7/11686378/fa19e512c22a/41467_2024_55365_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9da7/11686378/533d85377dc0/41467_2024_55365_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9da7/11686378/be29f21b019d/41467_2024_55365_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9da7/11686378/3b1a52374591/41467_2024_55365_Fig8_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9da7/11686378/8cb7b636b4a4/41467_2024_55365_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9da7/11686378/a2ba078bb5bc/41467_2024_55365_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9da7/11686378/3e59ec40cb23/41467_2024_55365_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9da7/11686378/3c51e96ea940/41467_2024_55365_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9da7/11686378/fa19e512c22a/41467_2024_55365_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9da7/11686378/533d85377dc0/41467_2024_55365_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9da7/11686378/be29f21b019d/41467_2024_55365_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9da7/11686378/3b1a52374591/41467_2024_55365_Fig8_HTML.jpg

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本文引用的文献

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Nature. 2024 May;629(8012):697-703. doi: 10.1038/s41586-024-07347-7. Epub 2024 Apr 24.
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Molecular basis for proofreading by the unique exonuclease domain of Family-D DNA polymerases.家族 D DNA 聚合酶独特的外切酶结构域校对的分子基础。
Nat Commun. 2023 Dec 14;14(1):8306. doi: 10.1038/s41467-023-44125-x.
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UCSF ChimeraX: Tools for structure building and analysis.UCSF ChimeraX：结构构建和分析工具。
Protein Sci. 2023 Nov;32(11):e4792. doi: 10.1002/pro.4792.
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Distinct RPA functions promote eukaryotic DNA replication initiation and elongation.不同的 RPA 功能促进真核 DNA 复制起始和延伸。
Nucleic Acids Res. 2023 Oct 27;51(19):10506-10518. doi: 10.1093/nar/gkad765.
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CST-Polα/Primase: the second telomere maintenance machine.CST-Polα/Primase：第二 telomere 维持机器。
Genes Dev. 2023 Jul 1;37(13-14):555-569. doi: 10.1101/gad.350479.123. Epub 2023 Jul 26.
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Mechanism of primer synthesis by Primase-Polymerases.引发酶-聚合酶合成引物的机制。
Curr Opin Struct Biol. 2023 Oct;82:102652. doi: 10.1016/j.sbi.2023.102652. Epub 2023 Jul 15.
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ssDNA accessibility of Rad51 is regulated by orchestrating multiple RPA dynamics.Rad51 的单链 DNA 可及性受调控多个 RPA 动力学的影响。
Nat Commun. 2023 Jun 30;14(1):3864. doi: 10.1038/s41467-023-39579-y.
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