ArticleThe Journal of biological chemistry2010
Lon protease quality control of presecretory proteins in Escherichia coli and its dependence on the SecB and DnaJ (Hsp40) chaperones.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 33 citations in OpenAlex.
- Mutations that confer resistance to sodium azide affect the levels of two physiological isoforms of SecA inMicrobiology (Reading, England) · 2026Article
- T6SS4 is heterogeneously expressed in Yersinia pseudotuberculosis and is a target for transcriptional and post-transcriptional regulation.PLoS pathogens · 2025Article
- Inactivation of the conserved protease LonA increases production of xylanase and amylase in Bacillus subtilis.Microbial cell factories · 2024Article
- Role of the FnIII domain associated with a cell wall-degrading enzyme cellobiosidase of Xanthomonas oryzae pv. oryzae.Molecular plant pathology · 2022Article
- Reduced ATP-dependent proteolysis of functional proteins during nutrient limitation speeds the return of microbes to a growth state.Science signaling · 2021Article
- Bacterial Hsp90 Facilitates the Degradation of Aggregation-Prone Hsp70-Hsp40 Substrates.Frontiers in molecular biosciences · 2021Article
- How Quality Control Systems AID Sec-Dependent Protein Translocation.Frontiers in molecular biosciences · 2021Review
- Plastid chaperone HSP90C guides precursor proteins to the SEC translocase for thylakoid transport.Journal of experimental botany · 2020Article
- Protein structure, amino acid composition and sequence determine proteome vulnerability to oxidation-induced damage.The EMBO journal · 2020Article
- Directed evolution of SecB chaperones toward toxin-antitoxin systems.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Isolating Escherichia coli strains for recombinant protein production.Cellular and molecular life sciences : CMLS · 2017Review
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- Multitasking SecB chaperones in bacteria.Frontiers in microbiology · 2014Review
- Arabidopsis J-protein J20 delivers the first enzyme of the plastidial isoprenoid pathway to protein quality control.The Plant cell · 2013Article
- TAC from Mycobacterium tuberculosis: a paradigm for stress-responsive toxin-antitoxin systems controlled by SecB-like chaperones.Cell stress & chaperones · 2013Article
- Hsp33 controls elongation factor-Tu stability and allows Escherichia coli growth in the absence of the major DnaK and trigger factor chaperones.The Journal of biological chemistry · 2012Article
- Chaperone-assisted excisive recombination, a solitary role for DnaJ (Hsp40) chaperone in lysogeny escape.The Journal of biological chemistry · 2011Article
- Conserved, disordered C terminus of DnaK enhances cellular survival upon stress and DnaK in vitro chaperone activity.The Journal of biological chemistry · 2011Article
- SecB-like chaperone controls a toxin-antitoxin stress-responsive system in Mycobacterium tuberculosis.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Various environmental insults result in irreversible damage to proteins and protein complexes. To cope, cells have evolved dedicated protein quality control mechanisms involving molecular chaperones and proteases. Here, we provide both genetic and biochemical evidence that the Lon protease and the SecB and DnaJ/Hsp40 chaperones are involved in the quality control of presecretory proteins in Escherichia coli. We showed that mutations in the lon gene alleviate the cold-sensitive phenotype of a secB mutant. Such suppression was not observed with either clpP or clpQ protease mutants. In comparison to the respective single mutants, the double secB lon mutant strongly accumulates aggregates of SecB substrates at physiological temperatures, suggesting that the chaperone and the protease share substrates. These observations were extended in vitro by showing that the main substrates identified in secB lon aggregates, namely proOmpF and proOmpC, are highly sensitive to specific degradation by Lon. In contrast, both substrates are significantly protected from Lon degradation by SecB. Interestingly, the chaperone DnaJ by itself protects substrates better from Lon degradation than SecB or the complete DnaK/DnaJ/GrpE chaperone machinery. In agreement with this finding, a DnaJ mutant protein that does not functionally interact in vivo with DnaK efficiently suppresses the SecB cold-sensitive phenotype, highlighting the role of DnaJ in assisting presecretory proteins. Taken together, our data suggest that when the Sec secretion pathway is compromised, a pool of presecretory proteins is transiently maintained in a translocation-competent state and, thus, protected from Lon degradation by either the SecB or DnaJ chaperones.
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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.