Anglia Ruskin Research Online (ARRO)
Browse
Parker_et_al_2021.pdf (2.61 MB)

The structure of the bacterial DNA segregation ATPase filament reveals the conformational plasticity of ParA upon DNA binding

Download (2.61 MB)
journal contribution
posted on 2023-07-26, 15:30 authored by Alexandra V. Parker, Daniel Mann, Svetomir B. Tzokov, Ling Chin Hwang, Julien R. C. Bergeron
The efficient segregation of replicated genetic material is an essential step for cell division. Bacterial cells use several evolutionarily-distinct genome segregation systems, the most common of which is the type I Par system. It consists of an adapter protein, ParB, that binds to the DNA cargo via interaction with the parS DNA sequence; and an ATPase, ParA, that binds nonspecific DNA and mediates cargo transport. However, the molecular details of how this system functions are not well understood. Here, we report the cryo-EM structure of the Vibrio cholerae ParA2 filament bound to DNA, as well as the crystal structures of this protein in various nucleotide states. These structures show that ParA forms a left-handed filament on DNA, stabilized by nucleotide binding, and that ParA undergoes profound structural rearrangements upon DNA binding and filament assembly. Collectively, our data suggest the structural basis for ParA’s cooperative binding to DNA and the formation of high ParA density regions on the nucleoid.

History

Refereed

  • Yes

Volume

12

Issue number

1

Page range

5166

Publication title

Nature Communications

ISSN

2041-1723

Publisher

Nature Research

File version

  • Published version

Language

  • eng

Legacy posted date

2021-09-21

Legacy creation date

2021-09-21

Legacy Faculty/School/Department

Faculty of Health, Education, Medicine & Social Care

Usage metrics

    ARU Outputs

    Categories

    No categories selected

    Licence

    Exports

    RefWorks
    BibTeX
    Ref. manager
    Endnote
    DataCite
    NLM
    DC