Self-organization of parS centromeres by the ParB CTP hydrolase.

Details

Serval ID
serval:BIB_9E013C97CC59
Type
Article: article from journal or magazin.
Collection
Publications
Title
Self-organization of parS centromeres by the ParB CTP hydrolase.
Journal
Science
Author(s)
Soh Y.M., Davidson I.F., Zamuner S., Basquin J., Bock F.P., Taschner M., Veening J.W., De Los Rios P., Peters J.M., Gruber S.
ISSN
1095-9203 (Electronic)
ISSN-L
0036-8075
Publication state
Published
Issued date
29/11/2019
Peer-reviewed
Oui
Volume
366
Number
6469
Pages
1129-1133
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Abstract
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.
Keywords
Bacillus subtilis/enzymology, Bacillus subtilis/genetics, Bacterial Proteins/chemistry, Bacterial Proteins/genetics, Centromere/enzymology, Cytidine Triphosphate/chemistry, Helix-Turn-Helix Motifs, Hydrolysis, Inverted Repeat Sequences, Protein Domains, Protein Multimerization, Pyrophosphatases/chemistry, Pyrophosphatases/genetics
Pubmed
Web of science
Create date
04/01/2020 12:33
Last modification date
03/05/2020 7:02
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