ArticleMolecular microbiology2019
Lon recognition of the replication initiator DnaA requires a bipartite degron.
Article in Molecular microbiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Proteomic survey of the DNA damage response inJournal of bacteriology · 2023Article
- Proteomic survey of the DNA damage response inbioRxiv : the preprint server for biology · 2023Article
- Degron-mediated proteolysis of CrhR-like DEAD-box RNA helicases in cyanobacteria.The Journal of biological chemistry · 2022Article
- Cryo-EM structure of the full-length Lon protease from Thermus thermophilus.FEBS letters · 2021Article
- Inorganic polyphosphate in host and microbe biology.Trends in microbiology · 2021Review
- A nascent polypeptide sequence modulates DnaA translation elongation in response to nutrient availability.eLife · 2021Article
- Applications of Bacterial Degrons and Degraders - Toward Targeted Protein Degradation in Bacteria.Frontiers in molecular biosciences · 2021Review
- Quantitative Proteome Profiling of aFrontiers in plant science · 2021Article
- Degradation of Lon in Caulobacter crescentus.Journal of bacteriology · 2020Article
- The Lon Protease Links Nucleotide Metabolism with Proteotoxic Stress.Molecular cell · 2020Article
- HdaB: a novel and conserved DnaA-related protein that targets the RIDA process to stimulate replication initiation.Nucleic acids research · 2020Article
- Article
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Authors and funding
4 authors.
Funding
Abstract
DnaA initiates chromosome replication in bacteria. In Caulobacter crescentus, the Lon protease degrades DnaA to coordinate replication with nutrient availability and to halt the cell cycle during acute stress. Here, we characterize the mechanism of DnaA recognition by Lon. We find that the folded state of DnaA appears crucial for its degradation, in contrast to the well-known role of Lon in degrading misfolded proteins. We fail to identify a single degradation motif (degron) sufficient for DnaA degradation, rather we show that both the ATPase domain and a species-specific N-terminal motif are important for productive Lon degradation of full-length DnaA. Mutations in either of these determinants disrupt DnaA degradation in vitro and in vivo. However, analysis of truncation products reveals that appending other extensions to the ATPase domain is sufficient to trigger degradation, suggesting plasticity in Lon recognition. Our final working model is that Lon engages DnaA through at least two elements, one of which anchors DnaA to Lon and the other acting as an initiation site for degradation.
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