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Title: | CryoEM structures of human CMG - ATPγS - DNA and CMG - AND-1 complexes |
Authors: | Rzechorzek, Neil J Hardwick, Steven W Jatikusumo, Vincentius A |
Keywords: | Cdc45-MCM-GINS (CMG); DNA |
Issue Date: | 2020 |
Publisher: | Biochemical Journal |
Abstract: | DNA unwinding in eukaryotic replication is performed by the Cdc45-MCM-GINS (CMG) helicase. Although the CMG architecture has been elucidated, its mechanism of DNA unwinding and replisome interactions remain poorly understood. Here we report the cryoEM structure at 3.3 Å of human CMG bound to fork DNA and the ATP-analogue ATPγS. Eleven nucleotides of single-stranded (ss) DNA are bound within the C-tier of MCM2-7 AAA+ ATPase domains. All MCM subunits contact DNA, from MCM2 at the 5′-end to MCM5 at the 3′-end of the DNA spiral, but only MCM6, 4, 7 and 3 make a full set of interactions. DNA binding correlates with nucleotide occupancy: five MCM subunits are bound to either ATPγS or ADP, whereas the apo MCM2-5 interface remains open. We further report the cryoEM structure of human CMG bound to the replisome hub AND-1 (CMGA). The AND-1 trimer uses one β-propeller domain of its trimerisation region to dock onto the side of the helicase assembly formed by Cdc45 and GINS. In the resulting CMGA architecture, the AND-1 trimer is closely positioned to the fork DNA while its CIP (Ctf4-interacting peptide)-binding helical domains remain available to recruit partner proteins. |
Description: | Tài liệu này được phát hành theo giấy phép CC-BY 4.0 |
URI: | http://dlib.hust.edu.vn/handle/HUST/24799 |
Link item primary: | https://www.biorxiv.org/content/10.1101/2020.01.22.914192v1 |
Appears in Collections: | OER - Kỹ thuật hóa học; Công nghệ sinh học - Thực phẩm; Công nghệ môi trường |
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