The CTPase activity of ParB determines the size and dynamics of prokaryotic DNA partition complexes
| Autor: | Laura Corrales-Guerrero, Wieland Steinchen, Chandan K. Das, Patrick H. Viollier, Marc Bramkamp, Seán M. Murray, Florian Altegoer, Martin Thanbichler, Lara Connolley, Helge Feddersen, Manuel Osorio-Valeriano, Giacomo Giacomelli, Juri Hanßmann, Gert Bange, Pietro Ivan Giammarinaro, Lars V. Schäfer, Gaël Panis |
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| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
DNA
Bacterial Myxococcus xanthus Time Factors NTPase Protein Conformation Cytidine Triphosphate Biology Crystallography X-Ray ParB/Srx domain Substrate Specificity Structure-Activity Relationship chemistry.chemical_compound Plasmid Bacterial Proteins Catalytic Domain Chromosome Segregation Centromere Nucleotide-binding protein Nucleotide ddc:610 Molecular Biology ParA ddc:616 chemistry.chemical_classification Binding Sites Hydrolysis Circular bacterial chromosome ParB-like nuclease domain Water wire Gene Expression Regulation Bacterial Cell Biology Chromosomes Bacterial biology.organism_classification Nucleotide hydrolysis Nucleoprotein chemistry Prokaryotic DNA replication Mutation ParB/sulfiredoxin domain Biophysics Nucleotide-binding site DNA |
| Zdroj: | 'Molecular Cell ', vol: 81, pages: 3992-4007 (2021) Molecular cell 81(19), 3992-4007.e10 (2021). doi:10.1016/j.molcel.2021.09.004 Molecular cell, Vol. 81, No 19 (2021) pp. 3992-4007.e10 Mol Cell |
| ISSN: | 1097-2765 |
| Popis: | Molecular cell 81(19), 3992 - 4007.e10 (2021). doi:10.1016/j.molcel.2021.09.004 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. Published by Elsevier, New York, NY |
| Databáze: | OpenAIRE |
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