ArticleThe Journal of biological chemistry2013
Dissection of the ATPase active site of P1 ParA reveals multiple active forms essential for plasmid partition.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 30 citations in OpenAlex.
- Article
- Mutational analysis of the F plasmid partitioning protein ParA reveals residues required for oligomerization and plasmid maintenance.Nucleic acids research · 2025Article
- Analysis of the Primary Pathogenic Bacteria in Abscess Disease of Musk Deer Using Metagenomic Approaches.Animals : an open access journal from MDPI · 2025Article
- A prophage competition element protects Salmonella from lysis.Cell host & microbe · 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
- Molecular Analysis of pSK1 par: A Novel Plasmid Partitioning System Encoded by Staphylococcal Multiresistance Plasmids.Journal of molecular biology · 2022Article
- 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
- Article
- The structure of the bacterial DNA segregation ATPase filament reveals the conformational plasticity of ParA upon DNA binding.Nature communications · 2021Article
- Nonspecific DNA binding by P1 ParA determines the distribution of plasmid partition and repressor activities.The Journal of biological chemistry · 2020Article
- Reconstitution and Coupling of DNA Replication and Segregation in a Biomimetic System.Chembiochem : a European journal of chemical biology · 2019Article
- A novel system of bacterial cell division arrest implicated in horizontal transmission of an integrative and conjugative element.PLoS genetics · 2019Article
- Two-step chromosome segregation in the stalked budding bacterium Hyphomonas neptunium.Nature communications · 2019Article
- Structures of maintenance of carboxysome distribution Walker-box McdA and McdB adaptor homologs.Nucleic acids research · 2019Article
- Bactofilin-mediated organization of the ParABS chromosome segregation system in Myxococcus xanthus.Nature communications · 2017Article
- Structures of partition protein ParA with nonspecific DNA and ParB effector reveal molecular insights into principles governing Walker-box DNA segregation.Genes & development · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The segregation, or partition, of bacterial plasmids is driven by the action of plasmid-encoded partition ATPases, which work to position plasmids inside the cell. The most common type of partition ATPase, generally called ParA, is represented by the P1 plasmid ParA protein. ParA interacts with P1 ParB (the site-specific DNA binding protein that recognizes the parS partition site), and interacts with the bacterial chromosome via an ATP-dependent nonspecific DNA binding activity. ParA also regulates expression of the par genes by acting as a transcriptional repressor. ParA requires ATP for multiple steps and in different ways during the partition process. Here, we analyze the properties of mutations in P1 ParA that are altered in a key lysine in the Walker A motif of the ATP binding site. Four different residues at this position (Lys, Glu, Gln, Arg) result in four different phenotypes in vivo. We focus particularly on the arginine substitution (K122R) because it results in a worse-than-null and dominant-negative phenotype called ParPD. We show that ParAK122R binds and hydrolyzes ATP, although the latter activity is reduced compared with wild-type. ParAK122R interacts with ParB, but the consequences of the interaction are damaged. The ability of ParB to stimulate the ATPase activity of ParA in vitro and its repressor activity in vivo is defective. The K122R mutation specifically damages the disassembly of ParA-ParB-DNA partition complexes, which we believe explains the ParPD phenotype in vivo.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.