ArticleMolecular microbiology2010
The IbpA and IbpB small heat-shock proteins are substrates of the AAA+ Lon protease.
Article in Molecular microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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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
37 citing papers in PubMed, 69 citations in OpenAlex.
- T6SS4 is heterogeneously expressed in Yersinia pseudotuberculosis and is a target for transcriptional and post-transcriptional regulation.PLoS pathogens · 2025Article
- Direct and indirect pathways linking the Lon protease to motility behaviors in the pathogen Pseudomonas aeruginosa.PLoS pathogens · 2025Article
- Maximally precise combinations to overcome metallo-β-lactamase-producingAntimicrobial agents and chemotherapy · 2024Article
- Global protein turnover quantification in Escherichia coli reveals cytoplasmic recycling under nitrogen limitation.Nature communications · 2024Article
- A review on oligomeric polydispersity and oligomers-dependent holding chaperone activity of the small heat-shock protein IbpB of Escherichia coli.Cell stress & chaperones · 2023Review
- Proteomic survey of the DNA damage response inJournal of bacteriology · 2023Article
- The Functionality of IbpA fromInternational journal of molecular sciences · 2023Article
- Article
- Proteomic survey of the DNA damage response inbioRxiv : the preprint server for biology · 2023Article
- Structure, Substrate Specificity and Role of Lon Protease in Bacterial Pathogenesis and Survival.International journal of molecular sciences · 2023Review
- New Insights into the Mechanism of Antibacterial Action of Synthetic PeptideAntibiotics (Basel, Switzerland) · 2022Article
- Shotgun Proteomics Revealed Preferential Degradation of Misfolded In Vivo Obligate GroE Substrates by Lon Protease inMolecules (Basel, Switzerland) · 2022Article
- Endogenous and Borrowed Proteolytic Activity in theMicrobiology and molecular biology reviews : MMBR · 2021Review
- The Small Ones Matter-sHsps in the Bacterial Chaperone Network.Frontiers in molecular biosciences · 2021Review
- Transcriptomic Analysis of Shiga Toxin-ProducingMicroorganisms · 2020Article
- N- and C-terminal regions of the small heat shock protein IbpA fromRSC advances · 2020Article
- Iron Limitation inFrontiers in microbiology · 2020Article
- Leveraging Peptide Substrate Libraries to Design Inhibitors of Bacterial Lon Protease.ACS chemical biology · 2019Article
- Duplicate divergence of two bacterial small heat shock proteins reduces the demand for Hsp70 in refolding of substrates.PLoS genetics · 2019Article
- N domain of the Lon AAA+ protease controls assembly and substrate choice.Protein science : a publication of the Protein Society · 2019Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Small heat-shock proteins (sHSPs) are a widely conserved family of molecular chaperones, all containing a conserved alpha-crystallin domain flanked by variable N- and C-terminal tails. We report that IbpA and IbpB, the sHSPs of Escherichia coli, are substrates for the AAA+ Lon protease. This ATP-fueled enzyme degraded purified IbpA substantially more slowly than purified IbpB, and we demonstrate that this disparity is a consequence of differences in maximal Lon degradation rates and not in substrate affinity. Interestingly, however, IbpB stimulated Lon degradation of IbpA both in vitro and in vivo. Furthermore, although the variable N- and C-terminal tails of the Ibps were dispensable for proteolytic recognition, these tails contain critical determinants that control the maximal rate of Lon degradation. Finally, we show that E. coli Lon degrades variants of human alpha-crystallin, indicating that Lon recognizes conserved determinants in the folded alpha-crystallin domain itself. These results suggest a novel mode for Lon substrate recognition and provide a highly suggestive link between the degradation and sHSP branches of the protein quality-control network.
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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.