Help Privacy Policy Disclaimer
  Advanced SearchBrowse




Journal Article

Self-organization of parS centromeres by the ParB CTP hydrolase


Basquin,  Jerome
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available

Soh, Y.-M., Davidson, I. F., Zamuner, S., Basquin, J., Bock, F. P., Taschner, M., et al. (2019). Self-organization of parS centromeres by the ParB CTP hydrolase. SCIENCE, 366(6469), 1129-1133. doi:10.1126/science.aay3965.

Cite as: https://hdl.handle.net/21.11116/0000-0005-9D70-C
ParABS systems facilitate chromosome segregation and plasmid partitioning in bacteria and archaea. ParB protein binds centromeric parS DNA sequences and spreads to flanking DNA. We show that ParB is an enzyme that hydrolyzes cytidine triphosphate (CTP) to cytidine diphosphate (CDP). parS DNA stimulates cooperative CTP binding by ParB and CTP hydrolysis. A nucleotide cocrystal structure elucidates the catalytic center of the dimerization-dependent ParB CTPase. Single-molecule imaging and biochemical assays recapitulate features of ParB spreading from parS in the presence but not absence of CTP. These findings suggest that centromeres assemble by self-loading of ParB DNA sliding clamps at parS. ParB CTPase is not related to known nucleotide hydrolases and might be a promising target for developing new classes of antibiotics.