ArticleProceedings of the National Academy of Sciences of the United States of America2018
Roles for ClpXP in regulating the circadian clock in
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
17 citing papers in PubMed, 30 citations in OpenAlex.
- From phenomenon to mechanism in the circadian clock of Synechococcus elongatus.Npj biological timing and sleep · 2026Review
- Effects of the signaling molecule cyclic-di-GMP on cyanobacterial circadian rhythm inJournal of bacteriology · 2026Article
- Cyanobacterial circadian regulation enhances bioproduction under subjective nighttime through rewiring of carbon partitioning dynamics, redox balance orchestration, and cell cycle modulation.Microbial cell factories · 2025Article
- Review
- Endogenous clock-mediated regulation of intracellular oxygen dynamics is essential for diazotrophic growth of unicellular cyanobacteria.Nature communications · 2024Article
- Genetics of conditional extended mycelial cell viability ofFrontiers in microbiology · 2024Article
- Synchronization of the circadian clock to the environment tracked in real time.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Glycogen metabolism is required for optimal cyanobacterial growth in the rapid light-dark cycle of low-Earth orbit.Life sciences in space research · 2023Article
- Comparative Genomics of Synechococcus elongatus Explains the Phenotypic Diversity of the Strains.mBio · 2022Article
- Degron-mediated proteolysis of CrhR-like DEAD-box RNA helicases in cyanobacteria.The Journal of biological chemistry · 2022Article
- Proteomic analysis of the regulatory networks of ClpX in a model cyanobacteriumFrontiers in plant science · 2022Article
- The lack of the cell division protein FtsZ induced generation of giant cells under acidic stress in cyanobacterium Synechocystis sp. PCC6803.Photosynthesis research · 2021Article
- Structural Determinants and Their Role in Cyanobacterial Morphogenesis.Life (Basel, Switzerland) · 2020Review
- Principles of rhythmicity emerging from cyanobacteria.The European journal of neuroscience · 2020Article
- Systematic Identification of Target Genes for Cellular Morphology Engineering inFrontiers in microbiology · 2020Article
- Molecular and structural insights into an asymmetric proteolytic complex (ClpP1P2) from Mycobacterium smegmatis.Scientific reports · 2019Article
- Structure, function, and substrates of Clp AAA+ protease systems in cyanobacteria, plastids, and apicoplasts: A comparative analysis.The Journal of biological chemistryReview
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
In cyanobacteria, the KaiABC posttranslational oscillator drives circadian rhythms of gene expression and controls the timing of cell division. The Kai-based oscillator can be reconstituted in vitro, demonstrating that the clock can run without protein synthesis and degradation; however, protein degradation is known to be important for clock function in vivo. Here, we report that strains deficient in the ClpXP1P2 protease have, in addition to known long-period circadian rhythms, an exaggerated ability to synchronize with the external environment (reduced "jetlag") compared with WT strains. Deletion of the ClpX chaperone, but not the protease subunits ClpP1 or ClpP2, results in cell division defects in a manner that is dependent on the expression of a dusk-peaking factor. We propose that chaperone activities of ClpX are required to coordinate clock control of cell division whereas the protease activities of the ClpXP1P2 complex are required to maintain appropriate periodicity of the clock and its synchronization with the external environment.
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Registered trials
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.