Journal Article

FZJ-2021-05158

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png The structure of the bacterial DNA segregation ATPase filament reveals the conformational plasticity of ParA upon DNA binding

Parker, A. ; Mann, D.FZJ* ; Tzokov, S. ; Hwang, L. ; Bergeron, C. (Corresponding author)

2021
Nature Publishing Group UK [London]

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Please use a persistent id in citations: http://hdl.handle.net/2128/30804  doi:10.1038/s41467-021-25429-2

Abstract: The efficient segregation of replicated genetic material is an essential step for cell division.Bacterial cells use several evolutionarily-distinct genome segregation systems, the mostcommon of which is the type I Par system. It consists of an adapter protein, ParB, that bindsto the DNA cargo via interaction with the parS DNA sequence; and an ATPase, ParA, thatbinds nonspecific DNA and mediates cargo transport. However, the molecular details of howthis system functions are not well understood. Here, we report the cryo-EM structure of theVibrio cholerae ParA2 filament bound to DNA, as well as the crystal structures of this proteinin various nucleotide states. These structures show that ParA forms a left-handed filament onDNA, stabilized by nucleotide binding, and that ParA undergoes profound structural rear-rangements upon DNA binding and filament assembly. Collectively, our data suggest thestructural basis for ParA’s cooperative binding to DNA and the formation of high ParA densityregions on the nucleoid.

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Contributing Institute(s):

1. Strukturbiologie (ER-C-3)

Research Program(s):

1. 5352 - Understanding the Functionality of Soft Matter and Biomolecular Systems (POF4-535) (POF4-535)
2. 5241 - Molecular Information Processing in Cellular Systems (POF4-524) (POF4-524)

Appears in the scientific report 2022

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