ArticleProceedings of the National Academy of Sciences of the United States of America2016
Caulobacter PopZ forms an intrinsically disordered hub in organizing bacterial cell poles.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
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Who cites it
66 citing papers in PubMed, 121 citations in OpenAlex.
- The polar landscape of bacterial pathogens and predators.Current opinion in microbiology · 2026Review
- CenIR, an essential BlaIR-family regulatory system inJournal of bacteriology · 2026Article
- CenIR, an essential BlaIR-family regulatory system inbioRxiv : the preprint server for biology · 2026Article
- The filamentous ultrastructure of the PopZ condensate is required for its cellular function.Nature structural & molecular biology · 2026Article
- Looking at bacterial cell poles from a liquid-liquid phase separation of intrinsically disordered proteins perspective.Current research in structural biology · 2025Article
- Mycobacterium tuberculosis uses intrinsically disordered, fast evolving proteins to interact with conserved host factors.Genome biology · 2025Article
- Electron Cryo-Tomography Reveals thebioRxiv : the preprint server for biology · 2025Article
- Phosphorylation of a conserved intrinsically disordered region is necessary for activation of a bacterial Hanks-type Ser/Thr kinase signaling pathway.bioRxiv : the preprint server for biology · 2025Article
- Multivalency Controls the Growth and Dynamics of a Biomolecular Condensate.Journal of the American Chemical Society · 2025Article
- Construction and phenotypic classification of synthetic dual-pole Escherichia coli cells.Communications biology · 2025Article
- De novo designed protein guiding targeted protein degradation.Nature communications · 2025Article
- Programming biological communication between distinct membraneless compartments.Nature chemical biology · 2025Article
- 'Intelligent' proteins.Cellular and molecular life sciences : CMLS · 2025Review
- Phase-Separated Multienzyme Condensates for Efficient Synthesis of Imines from Carboxylic Acids with Enhanced Dual-Cofactor Recycling.International journal of molecular sciences · 2025Article
- A CRISPR-SpCas9M-reporting system for efficient and rapid genome editing in Caulobacter crescentus.Nucleic acids research · 2025Article
- Manipulating subcellular protein localization to enhance target protein accumulation in minicells.Journal of biological engineering · 2025Article
- Phospho-signaling couples polar asymmetry and proteolysis within a membraneless microdomain in Caulobacter crescentus.Nature communications · 2024Article
- Biomolecular condensates as stress sensors and modulators of bacterial signaling.PLoS pathogens · 2024Review
- The Streptococcus phage protein paratox is an intrinsically disordered protein.Protein science : a publication of the Protein Society · 2024Article
- Three factors ParA, TipN, and DnaA-mediated chromosome replication initiation are contributors of centromere segregation inMolecular biology of the cell · 2024Article
6 more citing papers are in PubMed but not listed here.
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6 authors at 1 institution in 1 country.
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Abstract
Despite their relative simplicity, bacteria have complex anatomy at the subcellular level. At the cell poles of Caulobacter crescentus, a 177-amino acid (aa) protein called PopZ self-assembles into 3D polymeric superstructures. Remarkably, we find that this assemblage interacts directly with at least eight different proteins, which are involved in cell cycle regulation and chromosome segregation. The binding determinants within PopZ include 24 aa at the N terminus, a 32-aa region near the C-terminal homo-oligomeric assembly domain, and portions of an intervening linker region. Together, the N-terminal 133 aa of PopZ are sufficient for interacting with all binding partners, even in the absence of homo-oligomeric assembly. Structural analysis of this region revealed that it is intrinsically disordered, similar to p53 and other hub proteins that organize complex signaling networks in eukaryotic cells. Through live-cell photobleaching, we find rapid binding kinetics between PopZ and its partners, suggesting many pole-localized proteins become concentrated at cell poles through rapid cycles of binding and unbinding within the PopZ scaffold. We conclude that some bacteria, similar to their eukaryotic counterparts, use intrinsically disordered hub proteins for network assembly and subcellular organization.
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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.