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-Structure paper
タイトル | Cryo-EM structure and dynamics of eukaryotic DNA polymerase δ holoenzyme. |
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ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 26, Issue 10, Page 955-962, Year 2019 |
掲載日 | 2019年10月3日 |
著者 | Rinku Jain / William J Rice / Radhika Malik / Robert E Johnson / Louise Prakash / Satya Prakash / Iban Ubarretxena-Belandia / Aneel K Aggarwal / |
PubMed 要旨 | DNA polymerase δ (Polδ) plays pivotal roles in eukaryotic DNA replication and repair. Polδ is conserved from yeast to humans, and mutations in human Polδ have been implicated in various cancers. ...DNA polymerase δ (Polδ) plays pivotal roles in eukaryotic DNA replication and repair. Polδ is conserved from yeast to humans, and mutations in human Polδ have been implicated in various cancers. Saccharomyces cerevisiae Polδ consists of catalytic Pol3 and the regulatory Pol31 and Pol32 subunits. Here, we present the near atomic resolution (3.2 Å) cryo-EM structure of yeast Polδ holoenzyme in the act of DNA synthesis. The structure reveals an unexpected arrangement in which the regulatory subunits (Pol31 and Pol32) lie next to the exonuclease domain of Pol3 but do not engage the DNA. The Pol3 C-terminal domain contains a 4Fe-4S cluster and emerges as the keystone of Polδ assembly. We also show that the catalytic and regulatory subunits rotate relative to each other and that this is an intrinsic feature of the Polδ architecture. Collectively, the structure provides a framework for understanding DNA transactions at the replication fork. |
リンク | Nat Struct Mol Biol / PubMed:31582849 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.2 Å |
構造データ | EMDB-20235: Structure of a complex |
化合物 | ChemComp-SF4: ChemComp-DCP: ChemComp-CA: ChemComp-HOH: |
由来 |
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キーワード | dna binding protein/dna / DNA binding / enzyme / catalysis / regulation / DNA BINDING PROTEIN / dna binding protein-dna complex |