ArticleProceedings of the National Academy of Sciences of the United States of America2006
A phospho-signaling pathway controls the localization and activity of a protease complex critical for bacterial cell cycle progression.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 123 papers.
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Who cites it
123 citing papers in PubMed, 206 citations in OpenAlex.
- Disrupting NtrC function reveals unexpected robustness in a central cell cycle regulatory network.mBio · 2025Article
- Construction and phenotypic classification of synthetic dual-pole Escherichia coli cells.Communications biology · 2025Article
- Phospho-signaling couples polar asymmetry and proteolysis within a membraneless microdomain in Caulobacter crescentus.Nature communications · 2024Article
- ClpP protease modulates bacterial growth, stress response, and bacterial virulence in Brucella abortus.Veterinary research · 2023Article
- Asparagine Uptake: a Cellular Strategy ofApplied and environmental microbiology · 2023Article
- Turing-pattern model of scaffolding proteins that establish spatial asymmetry during the cell cycle ofiScience · 2023Article
- Structural features discriminating hybrid histidine kinase Rec domains from response regulator homologs.Nature communications · 2023Article
- Article
- Proteolysis dependent cell cycle regulation in Caulobacter crescentus.Cell division · 2022Review
- Modeling the temporal dynamics of master regulators and CtrA proteolysis in Caulobacter crescentus cell cycle.PLoS computational biology · 2022Article
- Computational modeling of unphosphorylated CtrA:iScience · 2021Article
- Activation of a signaling pathway by the physical translocation of a chromosome.Developmental cell · 2021Article
- Cargo competition for a dimerization interface restricts and stabilizes a bacterial protease adaptor.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- A localized adaptor protein performs distinct functions at theProceedings of the National Academy of Sciences of the United States of America · 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
- Programmed Proteolysis of Chemotaxis Proteins in Sinorhizobium meliloti: Features in the C-Terminal Region Control McpU Degradation.Journal of bacteriology · 2020Article
- Regulation of Bacterial Cell Cycle Progression by Redundant Phosphatases.Journal of bacteriology · 2020Article
- The type IV pilin PilA couples surface attachment and cell-cycle initiation inProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Integrative and quantitative view of the CtrA regulatory network in a stalked budding bacterium.PLoS genetics · 2020Article
- Article
63 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Temporally and spatially controlled master regulators drive the Caulobacter cell cycle by regulating the expression of >200 genes. Rapid clearance of the master regulator, CtrA, by the ClpXP protease is a critical event that enables the initiation of chromosome replication at specific times in the cell cycle. We show here that a previously unidentified single domain-response regulator, CpdR, when in the unphosphorylated state, binds to ClpXP and, thereby, causes its localization to the cell pole. We further show that ClpXP localization is required for CtrA proteolysis. When CpdR is phosphorylated, ClpXP is delocalized, and CtrA is not degraded. Both CtrA and CpdR are phosphorylated via the same CckA histidine kinase phospho-signaling pathway, providing a reinforcing mechanism that simultaneously activates CtrA and prevents its degradation by delocalizing the CpdR/ClpXP complex. In swarmer cells, CpdR is in the phosphorylated state, thus preventing ClpXP localization and CtrA degradation. As swarmer cells differentiate into stalked cells (G1/S transition), unphosphorylated CpdR accumulates and is localized to the stalked cell pole, where it enables ClpXP localization and CtrA proteolysis, allowing the initiation of DNA replication. Dynamic protease localization mediated by a phospho-signaling pathway is a novel mechanism to integrate spatial and temporal control of bacterial cell cycle progression.
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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.