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CTP and parS coordinate ParB partition complex dynamics and ParA-ATPase activation for ParABS-mediated DNA partitioning

James A. Taylor, Yeonee Seol, Jagat Budhathoki, View ORCID ProfileKeir C. Neuman, View ORCID ProfileKiyoshi Mizuuchi
doi: https://doi.org/10.1101/2021.01.24.427996
James A. Taylor
1Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
3Alzheimer’s Research UK Oxford Drug Discovery Institute, University of Oxford
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Yeonee Seol
2Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health
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Jagat Budhathoki
1Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
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Keir C. Neuman
2Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health
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Kiyoshi Mizuuchi
1Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
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  • ORCID record for Kiyoshi Mizuuchi
  • For correspondence: kiyoshimi@niddk.nih.gov
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Abstract

ParABS partition systems, comprising the centromere-like DNA sequence parS, the parS-binding ParB-CTPase and the nucleoid-binding ParA-ATPase, ensure faithful segregation of bacterial chromosomes and low-copy-number plasmids. F-plasmid partition complexes containing ParBF and parSF move by generating and following a local concentration gradient of nucleoid-bound ParAF. However, the process through which ParBF activates ParAF-ATPase has not been defined. We studied CTP- and parSF-modulated ParAF—ParBF complex assembly, in which DNA-bound ParAF-ATP dimers are activated for ATP hydrolysis by interacting with two ParBF N-terminal domains. CTP or parSF enhances the ATPase rate without significantly accelerating ParAF—ParBF complex assembly. Together, parSF and CTP accelerate ParAF—ParBF assembly without further significant increase in ATPase rate. Magnetic-tweezers experiments showed that CTP promotes multiple ParBF loading onto parSF-containing DNA, generating condensed partition complex-like assemblies. We propose that ParBF in the partition complex adopts a conformation that enhances ParBF—ParBF and ParAF—ParBF interactions promoting efficient partitioning.

Competing Interest Statement

The authors have declared no competing interest.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-ND 4.0 International license.
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Posted July 10, 2021.
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CTP and parS coordinate ParB partition complex dynamics and ParA-ATPase activation for ParABS-mediated DNA partitioning
James A. Taylor, Yeonee Seol, Jagat Budhathoki, Keir C. Neuman, Kiyoshi Mizuuchi
bioRxiv 2021.01.24.427996; doi: https://doi.org/10.1101/2021.01.24.427996
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CTP and parS coordinate ParB partition complex dynamics and ParA-ATPase activation for ParABS-mediated DNA partitioning
James A. Taylor, Yeonee Seol, Jagat Budhathoki, Keir C. Neuman, Kiyoshi Mizuuchi
bioRxiv 2021.01.24.427996; doi: https://doi.org/10.1101/2021.01.24.427996

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