TY  - JOUR
AU  - Parker, AV
AU  - Mann, Daniel
AU  - Tzokov, SB
AU  - Hwang, LC
AU  - Bergeron, C.
TI  - The structure of the bacterial DNA segregation ATPase filament reveals the conformational plasticity of ParA upon DNA binding
JO  - Nature Communications
VL  - 12
SN  - 2041-1723
CY  - [London]
PB  - Nature Publishing Group UK
M1  - FZJ-2021-05158
SP  - 5166
PY  - 2021
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - pmid:34453062
UR  - <Go to ISI:>//WOS:000691020900009
DO  - DOI:10.1038/s41467-021-25429-2
UR  - https://juser.fz-juelich.de/record/903486
ER  -