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Lookup NU author(s): Dr Simone PelliciariORCiD, Dr Stepan Fenyk, Dr Daniel Stevens, Dr Charles WinterhalterORCiD, Dr Frederic SchrammORCiD, Sara Pintar, George Merces, Dr Tom Richardson, Dr Julia Hubbard, Professor Heath MurrayORCiD
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
© 2023, The Author(s).Genome duplication is essential for the proliferation of cellular life and this process is generally initiated by dedicated replication proteins at chromosome origins. In bacteria, DNA replication is initiated by the ubiquitous DnaA protein, which assembles into an oligomeric complex at the chromosome origin (oriC) that engages both double-stranded DNA (dsDNA) and single-stranded DNA (ssDNA) to promote DNA duplex opening. However, the mechanism of DnaA specifically opening a replication origin was unknown. Here we show that Bacillus subtilis DnaAATP assembles into a continuous oligomer at the site of DNA melting, extending from a dsDNA anchor to engage a single DNA strand. Within this complex, two nucleobases of each ssDNA binding motif (DnaA-trio) are captured within a dinucleotide binding pocket created by adjacent DnaA proteins. These results provide a molecular basis for DnaA specifically engaging the conserved sequence elements within the bacterial chromosome origin basal unwinding system (BUS).
Author(s): Pelliciari S, Bodet-Lefevre S, Fenyk S, Stevens D, Winterhalter C, Schramm FD, Pintar S, Burnham DR, Merces G, Richardson TT, Tashiro Y, Hubbard J, Yardimci H, Ilangovan A, Murray H
Publication type: Article
Publication status: Published
Journal: Nature Communications
Year: 2023
Volume: 14
Issue: 1
Online publication date: 14/12/2023
Acceptance date: 21/11/2023
Date deposited: 18/01/2024
ISSN (electronic): 2041-1723
Publisher: Nature Research
URL: https://doi.org/10.1038/s41467-023-43823-w
DOI: 10.1038/s41467-023-43823-w
Data Access Statement: The previously published X-ray data used in this study are available in the PDB database under accession code 3R8F. The cryo-electron microscopy data generated in this study have been deposited in the Electron Microscopy Data Bank under accession codes EMD-16230 (domain III lattice), EMD-16231 (dsDNA region), EMD-16256 (domain IV lattice), and EMD-16229 (overall map). The X-ray data generated in this study is available in the PDB database under accession code 8BV3. The structural model of the BUS complex generated in this study has been deposited in the PDB database under accession code 8BTG. Source data are provided with this paper.
PubMed id: 38097584
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