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The CTPase activity of ParB determines the size and dynamics of prokaryotic DNA partition complexes.
- Source :
-
Molecular cell [Mol Cell] 2021 Oct 07; Vol. 81 (19), pp. 3992-4007.e10. Date of Electronic Publication: 2021 Sep 24. - Publication Year :
- 2021
-
Abstract
- ParB-like CTPases mediate the segregation of bacterial chromosomes and low-copy number plasmids. They act as DNA-sliding clamps that are loaded at parS motifs in the centromere of target DNA molecules and spread laterally to form large nucleoprotein complexes serving as docking points for the DNA segregation machinery. Here, we solve crystal structures of ParB in the pre- and post-hydrolysis state and illuminate the catalytic mechanism of nucleotide hydrolysis. Moreover, we identify conformational changes that underlie the CTP- and parS-dependent closure of ParB clamps. The study of CTPase-deficient ParB variants reveals that CTP hydrolysis serves to limit the sliding time of ParB clamps and thus drives the establishment of a well-defined ParB diffusion gradient across the centromere whose dynamics are critical for DNA segregation. These findings clarify the role of the ParB CTPase cycle in partition complex assembly and function and thus advance our understanding of this prototypic CTP-dependent molecular switch.<br />Competing Interests: Declaration of interests The authors declare no competing interests.<br /> (Copyright © 2021 The Author(s). Published by Elsevier Inc. All rights reserved.)
- Subjects :
- Bacterial Proteins genetics
Binding Sites
Catalytic Domain
Crystallography, X-Ray
DNA, Bacterial genetics
Gene Expression Regulation, Bacterial
Hydrolysis
Mutation
Myxococcus xanthus genetics
Protein Conformation
Structure-Activity Relationship
Substrate Specificity
Time Factors
Bacterial Proteins metabolism
Chromosome Segregation
Chromosomes, Bacterial
Cytidine Triphosphate metabolism
DNA, Bacterial metabolism
Myxococcus xanthus enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 1097-4164
- Volume :
- 81
- Issue :
- 19
- Database :
- MEDLINE
- Journal :
- Molecular cell
- Publication Type :
- Academic Journal
- Accession number :
- 34562373
- Full Text :
- https://doi.org/10.1016/j.molcel.2021.09.004