ArticleNucleic acids research2013
Insight into centromere-binding properties of ParB proteins: a secondary binding motif is essential for bacterial genome maintenance.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 34 citations in OpenAlex.
- The ParB-CTP cycle activates phase separation in bacterial DNA segregation.Nucleic acids research · 2025Article
- DNA Segregation in Enterobacteria.EcoSal Plus · 2023Review
- Physical Modeling of a Sliding Clamp Mechanism for the Spreading of ParB at Short Genomic Distance from Bacterial Centromere Sites.iScience · 2020Article
- Deacetylation enhances ParB-DNA interactions affecting chromosome segregation in Streptomyces coelicolor.Nucleic acids research · 2020Article
- Spo0J and SMC are required for normal chromosome segregation in Staphylococcus aureus.MicrobiologyOpen · 2020Article
- Addressing the role of centromere sites in activation of ParB proteins for partition complex assembly.PloS one · 2020Article
- Plasmid Localization and Partition inEcoSal Plus · 2019Review
- A conserved mechanism drives partition complex assembly on bacterial chromosomes and plasmids.Molecular systems biology · 2018Article
- Article
- Segrosome Complex Formation during DNA Trafficking in Bacterial Cell Division.Frontiers in molecular biosciences · 2016Review
- ParB Partition Proteins: Complex Formation and Spreading at Bacterial and Plasmid Centromeres.Frontiers in molecular biosciences · 2016Review
- Replication and Active Partition of Integrative and Conjugative Elements (ICEs) of the SXT/R391 Family: The Line between ICEs and Conjugative Plasmids Is Getting Thinner.PLoS genetics · 2015Article
- Insights into ParB spreading from the complex structure of Spo0J and parS.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- A propagating ATPase gradient drives transport of surface-confined cellular cargo.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Defining the role of ATP hydrolysis in mitotic segregation of bacterial plasmids.PLoS genetics · 2013Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ParB proteins are one of the three essential components of partition systems that actively segregate bacterial chromosomes and plasmids. In binding to centromere sequences, ParB assembles as nucleoprotein structures called partition complexes. These assemblies are the substrates for the partitioning process that ensures DNA molecules are segregated to both sides of the cell. We recently identified the sopC centromere nucleotides required for binding to the ParB homologue of plasmid F, SopB. This analysis also suggested a role in sopC binding for an arginine residue, R219, located outside the helix-turn-helix (HTH) DNA-binding motif previously shown to be the only determinant for sopC-specific binding. Here, we demonstrated that the R219 residue is critical for SopB binding to sopC during partition. Mutating R219 to alanine or lysine abolished partition by preventing partition complex assembly. Thus, specificity of SopB binding relies on two distinct motifs, an HTH and an arginine residue, which define a split DNA-binding domain larger than previously thought. Bioinformatic analysis over a broad range of chromosomal ParBs generalized our findings with the identification of a non-HTH positively charged residue essential for partition and centromere binding, present in a newly identified highly conserved motif. We propose that ParB proteins possess two DNA-binding motifs that form an extended centromere-binding domain, providing high specificity.
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