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-Structure paper
タイトル | Cryo-EM structure of the replisome reveals multiple interactions coordinating DNA synthesis. |
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ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 114, Issue 10, Page E1848-E1856, Year 2017 |
掲載日 | 2017年3月7日 |
著者 | Arkadiusz W Kulczyk / Arne Moeller / Peter Meyer / Piotr Sliz / Charles C Richardson / |
PubMed 要旨 | We present a structure of the ∼650-kDa functional replisome of bacteriophage T7 assembled on DNA resembling a replication fork. A structure of the complex consisting of six domains of DNA helicase, ...We present a structure of the ∼650-kDa functional replisome of bacteriophage T7 assembled on DNA resembling a replication fork. A structure of the complex consisting of six domains of DNA helicase, five domains of RNA primase, two DNA polymerases, and two thioredoxin (processivity factor) molecules was determined by single-particle cryo-electron microscopy. The two molecules of DNA polymerase adopt a different spatial arrangement at the replication fork, reflecting their roles in leading- and lagging-strand synthesis. The structure, in combination with biochemical data, reveals molecular mechanisms for coordination of leading- and lagging-strand synthesis. Because mechanisms of DNA replication are highly conserved, the observations are relevant to other replication systems. |
リンク | Proc Natl Acad Sci U S A / PubMed:28223502 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 13.8 Å |
構造データ | EMDB-8565: |
由来 |
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