ArticleMolecular microbiology2013
Oligomerization and higher-order assembly contribute to sub-cellular localization of a bacterial scaffold.
Article in Molecular microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- A tunable aqueous architecture modulates functional output in biomolecular condensates.bioRxiv : the preprint server for biology · 2026Article
- The filamentous ultrastructure of the PopZ condensate is required for its cellular function.Nature structural & molecular biology · 2026Article
- The Microbial Anti-Inflammatory Molecule (MAM) is a key protein processed and exported toGut microbes · 2025Article
- Multivalency Controls the Growth and Dynamics of a Biomolecular Condensate.Journal of the American Chemical Society · 2025Article
- Phospho-signaling couples polar asymmetry and proteolysis within a membraneless microdomain in Caulobacter crescentus.Nature communications · 2024Article
- Diffusiophoresis promotes phase separation and transport of biomolecular condensates.Nature communications · 2024Article
- Three factors ParA, TipN, and DnaA-mediated chromosome replication initiation are contributors of centromere segregation inMolecular biology of the cell · 2024Article
- Distinct dynamics and proximity networks of hub proteins at the prey-invading cell pole in a predatory bacterium.Journal of bacteriology · 2024Article
- Diffusiophoresis promotes phase separation and transport of biomolecular condensates.bioRxiv : the preprint server for biology · 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
- Diffusiophoresis promotes phase separation and transport of biomolecular condensates.Research square · 2023Article
- The material properties of a bacterial-derived biomolecular condensate tune biological function in natural and synthetic systems.Nature communications · 2022Article
- Review
- ATP-responsive biomolecular condensates tune bacterial kinase signaling.Science advances · 2022Article
- Genus-Specific Interactions of Bacterial Chromosome Segregation Machinery Are Critical for Their Function.Frontiers in microbiology · 2022Article
- Catching a Walker in the Act-DNA Partitioning by ParA Family of Proteins.Frontiers in microbiology · 2022Review
- VirB, a key transcriptional regulator of virulence plasmid genes inJournal of bacteriology · 2021Article
- Intrinsically Disordered Bacterial Polar Organizing Protein Z, PopZ, Interacts with Protein Binding Partners Through an N-terminal Molecular Recognition Feature.Journal of molecular biology · 2020Article
- Cryogenic single-molecule fluorescence annotations for electron tomography reveal in situ organization of key proteins inProceedings of the National Academy of Sciences of the United States of America · 2020Article
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Authors and funding
7 authors.
Funding
Abstract
In Caulobacter crescentus, the PopZ polar scaffold protein supports asymmetric cell division by recruiting distinct sets of binding partners to opposite cell poles. To understand how polar organizing centres are established by PopZ, we investigated a set of mutated PopZ proteins for defects in sub-cellular localization and recruitment activity. We identified a domain within the C-terminal 76 amino acids that is necessary and sufficient for accumulation as a single subcellular focus, a domain within the N-terminal 23 amino acids that is necessary for bipolar targeting, and a linker domain between these localization determinants that tolerates large variation. Mutations that inhibited dynamic PopZ localization inhibited the recruitment of other factors to cell poles. Mutations in the C-terminal domain also blocked discrete steps in the assembly of higher-order structures. Biophysical analysis of purified wild type and assembly defective mutant proteins indicates that PopZ self-associates into an elongated trimer, which readily forms a dimer of trimers through lateral contact. The final six amino acids of PopZ are necessary for connecting the hexamers into filaments, and these structures are important for sub-cellular localization. Thus, PopZ undergoes multiple orders of self-assembly, and the formation of an interconnected superstructure is a key feature of polar organization in Caulobacter.
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