%0 Journal Article
%A Parker, AV
%A Mann, Daniel
%A Tzokov, SB
%A Hwang, LC
%A Bergeron, C.
%T The structure of the bacterial DNA segregation ATPase filament reveals the conformational plasticity of ParA upon DNA binding
%J Nature Communications
%V 12
%@ 2041-1723
%C [London]
%I Nature Publishing Group UK
%M FZJ-2021-05158
%P 5166
%D 2021
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:34453062
%U <Go to ISI:>//WOS:000691020900009
%R 10.1038/s41467-021-25429-2
%U https://juser.fz-juelich.de/record/903486