ArticleProceedings of the National Academy of Sciences of the United States of America2014
Cell cycle-dependent adaptor complex for ClpXP-mediated proteolysis directly integrates phosphorylation and second messenger signals.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
- Dynamic Executors of Bacterial Signals: Functional Versatility and Regulatory Networks of c-di-GMP Effectors.Biomolecules · 2025Review
- Phospho-signaling couples polar asymmetry and proteolysis within a membraneless microdomain in Caulobacter crescentus.Nature communications · 2024Article
- TheAnnual review of microbiology · 2023Review
- Evolution of cyclic di-GMP signalling on a short and long term time scale.Microbiology (Reading, England) · 2023Article
- Polarity of c-di-GMP synthesis and degradation.microLife · 2023Review
- Article
- ATP hydrolysis tunes specificity of a AAA+ protease.Cell reports · 2022Article
- 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
- 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
- Cell cycle control and environmental response by second messengers in Caulobacter crescentus.BMC bioinformatics · 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
- DNA and Polyphosphate in Directed Proteolysis for DNA Replication Control.Frontiers in microbiology · 2020Review
- Periplasmic protein EipA determines envelope stress resistance and virulence in Brucella abortus.Molecular microbiology · 2019Article
- Multilayered control of chromosome replication inBiochemical Society transactions · 2019Review
- Polar Localization Hub Protein PopZ Restrains Adaptor-Dependent ClpXP Proteolysis in Caulobacter crescentus.Journal of bacteriology · 2018Article
- Regulated Proteolysis in Bacteria.Annual review of biochemistry · 2018Review
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Authors and funding
7 authors.
Funding
Abstract
The cell-division cycle of Caulobacter crescentus depends on periodic activation and deactivation of the essential response regulator CtrA. Although CtrA is critical for transcription during some parts of the cell cycle, its activity must be eliminated before chromosome replication because CtrA also blocks the initiation of DNA replication. CtrA activity is down-regulated both by dephosphorylation and by proteolysis, mediated by the ubiquitous ATP-dependent protease ClpXP. Here we demonstrate that proteins needed for rapid CtrA proteolysis in vivo form a phosphorylation-dependent and cyclic diguanylate (cdG)-dependent adaptor complex that accelerates CtrA degradation in vitro by ClpXP. The adaptor complex includes CpdR, a single-domain response regulator; PopA, a cdG-binding protein; and RcdA, a protein whose activity cannot be predicted. When CpdR is unphosphorylated and when PopA is bound to cdG, they work together with RcdA in an all-or-none manner to reduce the Km of CtrA proteolysis 10-fold. We further identified a set of amino acids in the receiver domain of CtrA that modulate its adaptor-mediated degradation in vitro and in vivo. Complex formation between PopA and CtrA depends on these amino acids, which reside on alpha-helix 1 of the CtrA receiver domain, and on cdG binding by PopA. These results reveal that each accessory factor plays an essential biochemical role in the regulated proteolysis of CtrA and demonstrate, to our knowledge, the first example of a multiprotein, cdG-dependent proteolytic adaptor.
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