ArticleProceedings of the National Academy of Sciences of the United States of America2013
Critical clamp loader processing by an essential AAA+ protease in Caulobacter crescentus.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
29 citing papers in PubMed, 51 citations in OpenAlex.
- How the double-ring ClpAP protease motor grips the substrate to unfold and degrade stable proteins.The Journal of biological chemistry · 2024Article
- Slippery sequences stall the 26S proteasome at multiple points along the translocation pathway.Protein science : a publication of the Protein Society · 2024Article
- Proteomic survey of the DNA damage response inJournal of bacteriology · 2023Article
- AAA+ protease-adaptor structures reveal altered conformations and ring specialization.Nature structural & molecular biology · 2022Article
- Structure and function of ClpXP, a AAA+ proteolytic machine powered by probabilistic ATP hydrolysis.Critical reviews in biochemistry and molecular biology · 2022Review
- Proteolysis dependent cell cycle regulation in Caulobacter crescentus.Cell division · 2022Review
- Protein degradation control and regulation of bacterial survival and pathogenicity: the role of protein degradation systems in bacteria.Molecular biology reports · 2021Review
- The Protein Quality Control Network inFrontiers in molecular biosciences · 2021Review
- Multistep substrate binding and engagement by the AAA+ ClpXP protease.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The Mouse Heart Mitochondria N Terminome Provides Insights into ClpXP-Mediated Proteolysis.Molecular & cellular proteomics : MCP · 2020Article
- Heat-shock proteases promote survival ofProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Mitochondrial ClpX activates an essential biosynthetic enzyme through partial unfolding.eLife · 2020Article
- DNA and Polyphosphate in Directed Proteolysis for DNA Replication Control.Frontiers in microbiology · 2020Review
- Article
- Regulated Proteolysis in Bacteria.Annual review of biochemistry · 2018Review
- The Protease ClpXP and the PAS Domain Protein DivL Regulate CtrA and Gene Transfer Agent Production in Rhodobacter capsulatus.Applied and environmental microbiology · 2018Article
- The Essential Role of ClpXP inFrontiers in molecular biosciences · 2017Article
- Protease regulation and capacity during Caulobacter growth.Current opinion in microbiology · 2016Review
- Regulated Proteolysis in Bacteria: Caulobacter.Annual review of genetics · 2016Review
- Ribosomal frameshifting and transcriptional slippage: From genetic steganography and cryptography to adventitious use.Nucleic acids research · 2016Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Chromosome replication relies on sliding clamps that are loaded by energy-dependent complexes. In Escherichia coli, the ATP-binding clamp loader subunit DnaX exists as both long (τ) and short (γ) forms generated through programmed translational frameshifting, but the need for both forms is unclear. Here, we show that in Caulobacter crescentus, DnaX isoforms are unexpectedly generated through partial proteolysis by the AAA+ protease casein lytic proteinase (Clp) XP. We find that the normally processive ClpXP protease partially degrades DnaX to produce stable fragments upon encountering a glycine-rich region adjacent to a structured domain. Increasing the sequence complexity of this region prevents partial proteolysis and generates a τ-only form of DnaX in vivo that is unable to support viability on its own. Growth is restored when γ is provided in trans, but these strains are more sensitive to DNA damage compared with strains that can generate γ through proteolysis. Our work reveals an unexpected mode of partial processing by the ClpXP protease to generate DnaX isoforms, demonstrates that both τ and γ forms of DnaX are required for Caulobacter viability, and identifies a role for clamp loader diversity in responding to DNA damage. The conservation of distinct DnaX isoforms throughout bacteria despite fundamentally different mechanisms for producing them suggests there may be a conserved need for alternate clamp loader complexes during DNA damaging conditions.
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What OpenQuestion holds
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.