ArticleNucleic acids research2020
Molecular architecture of the DNA-binding sites of the P-loop ATPases MipZ and ParA from Caulobacter crescentus.
Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 34 citations in OpenAlex.
- Article
- Molecular basis of ParA ATPase activation by the CTPase ParB during bacterial chromosome segregation.Nature communications · 2025Article
- DNA supercoiling enhances DNA condensation by ParB proteins.Nucleic acids research · 2024Article
- Phase-separated ParB enforces diverse DNA compaction modes and stabilizes the parS-centered partition complex.Nucleic acids research · 2024Article
- Insights into the molecular mechanism of ParABS system in chromosome partition by HpParA and HpParB.Nucleic acids research · 2024Article
- Three factors ParA, TipN, and DnaA-mediated chromosome replication initiation are contributors of centromere segregation inMolecular biology of the cell · 2024Article
- TipN's involvement with centromere segregation in Caulobacter crescentus.bioRxiv : the preprint server for biology · 2023Article
- To let go or not to let go: how ParA can impact the release of the chromosomal anchoring in Caulobacter crescentus.Nucleic acids research · 2023Article
- Diverse Partners of the Partitioning ParB Protein in Pseudomonas aeruginosa.Microbiology spectrum · 2023Article
- Mass Spectrometry for Assessing Protein-Nucleic Acid Interactions.Analytical chemistry · 2023Review
- MipZ caps the plus-end of FtsZ polymers to promote their rapid disassembly.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Advances in Hydrogen/Deuterium Exchange Mass Spectrometry and the Pursuit of Challenging Biological Systems.Chemical reviews · 2022Review
- Catching a Walker in the Act-DNA Partitioning by ParA Family of Proteins.Frontiers in microbiology · 2022Review
- Dissection of the ATPase active site of McdA reveals the sequential steps essential for carboxysome distribution.Molecular biology of the cell · 2021Article
- Activation of a signaling pathway by the physical translocation of a chromosome.Developmental cell · 2021Article
- Hydrogen-deuterium exchange reveals a dynamic DNA-binding map of replication protein A.Nucleic acids research · 2021Article
- Bacterial chromosome segregation by the ParABS system.Open biology · 2020Review
- Rules and Exceptions: The Role of Chromosomal ParB in DNA Segregation and Other Cellular Processes.Microorganisms · 2020Review
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The spatiotemporal regulation of chromosome segregation and cell division in Caulobacter crescentus is mediated by two different P-loop ATPases, ParA and MipZ. Both of these proteins form dynamic concentration gradients that control the positioning of regulatory targets within the cell. Their proper localization depends on their nucleotide-dependent cycling between a monomeric and a dimeric state and on the ability of the dimeric species to associate with the nucleoid. In this study, we use a combination of genetic screening, biochemical analysis and hydrogen/deuterium exchange mass spectrometry to comprehensively map the residues mediating the interactions of MipZ and ParA with DNA. We show that MipZ has non-specific DNA-binding activity that relies on an array of positively charged and hydrophobic residues lining both sides of the dimer interface. Extending our analysis to ParA, we find that the MipZ and ParA DNA-binding sites differ markedly in composition, although their relative positions on the dimer surface and their mode of DNA binding are conserved. In line with previous experimental work, bioinformatic analysis suggests that the same principles may apply to other members of the P-loop ATPase family. P-loop ATPases thus share common mechanistic features, although their functions have diverged considerably during the course of evolution.
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