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Self-organization of parS centromeres by the ParB CTP hydrolase.
- Source :
-
Science (New York, N.Y.) [Science] 2019 Nov 29; Vol. 366 (6469), pp. 1129-1133. Date of Electronic Publication: 2019 Oct 24. - Publication Year :
- 2019
-
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.<br /> (Copyright © 2019 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.)
- Subjects :
- Bacillus subtilis genetics
Bacterial Proteins genetics
Helix-Turn-Helix Motifs
Hydrolysis
Inverted Repeat Sequences
Protein Domains
Protein Multimerization
Pyrophosphatases genetics
Bacillus subtilis enzymology
Bacterial Proteins chemistry
Centromere enzymology
Cytidine Triphosphate chemistry
Pyrophosphatases chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1095-9203
- Volume :
- 366
- Issue :
- 6469
- Database :
- MEDLINE
- Journal :
- Science (New York, N.Y.)
- Publication Type :
- Academic Journal
- Accession number :
- 31649139
- Full Text :
- https://doi.org/10.1126/science.aay3965