Ontology highlight
ABSTRACT:
SUBMITTER: Soh YM
PROVIDER: S-EPMC6927813 | biostudies-literature | 2019 Nov
REPOSITORIES: biostudies-literature
Soh Young-Min YM Davidson Iain Finley IF Zamuner Stefano S Basquin Jérôme J Bock Florian Patrick FP Taschner Michael M Veening Jan-Willem JW De Los Rios Paolo P Peters Jan-Michael JM Gruber Stephan S
Science (New York, N.Y.) 20191024 6469
ParABS systems facilitate chromosome segregation and plasmid partitioning in bacteria and archaea. ParB protein binds centromeric <i>parS</i> DNA sequences and spreads to flanking DNA. We show that ParB is an enzyme that hydrolyzes cytidine triphosphate (CTP) to cytidine diphosphate (CDP). <i>parS</i> 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 imagin ...[more]