ArticleProceedings of the National Academy of Sciences of the United States of America2007
Trigger Factor can antagonize both SecB and DnaK/DnaJ chaperone functions in Escherichia coli.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 75 citations in OpenAlex.
- Tripleknock: predicting lethal effect of three-gene knockout in bacteria by deep learning.Scientific reports · 2026Article
- Effect of the Bacterial Chaperones SecB and Trigger Factor (TF) on the Folding Dynamics and In Vitro Translocation of Cytoplasmic and Secretory Model Proteins.International journal of molecular sciences · 2025Article
- Ribosome profiling reveals multiple roles of SecA in cotranslational protein export.Nature communications · 2022Article
- Update on the Protein Homeostasis Network inFrontiers in microbiology · 2022Review
- The DisorderedMicroorganisms · 2021Article
- How Quality Control Systems AID Sec-Dependent Protein Translocation.Frontiers in molecular biosciences · 2021Review
- Trigger factor is a bona fide secretory pathway chaperone that interacts with SecB and the translocase.EMBO reports · 2020Article
- Structural insights into chaperone addiction of toxin-antitoxin systems.Nature communications · 2019Article
- Cold adaptation in the environmental bacteriumCommunications biology · 2019Article
- Comparative analysis of homologous aminopeptidase PepN from pathogenic and non-pathogenic mycobacteria reveals divergent traits.PloS one · 2019Article
- The way is the goal: how SecA transports proteins across the cytoplasmic membrane in bacteria.FEMS microbiology letters · 2018Review
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- Directed evolution of SecB chaperones toward toxin-antitoxin systems.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The chaperone toolbox at the single-molecule level: From clamping to confining.Protein science : a publication of the Protein Society · 2017Review
- System analysis of salt and osmotic stress induced proteins inJournal, genetic engineering & biotechnology · 2017Article
- SecA Cotranslationally Interacts with Nascent Substrate Proteins In Vivo.Journal of bacteriology · 2017Article
- Determination of the intracellular concentration of the export chaperone SecB in Escherichia coli.PloS one · 2017Article
- Protein export through the bacterial Sec pathway.Nature reviews. Microbiology · 2017Review
- Chaperone addiction of toxin-antitoxin systems.Nature communications · 2016Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Polypeptides emerging from the ribosome are assisted by a pool of molecular chaperones and targeting factors, which enable them to efficiently partition as cytoplasmic, integral membrane, or exported proteins. In Escherichia coli, the chaperones SecB, Trigger Factor (TF), and DnaK are key players in this process. Here, we report that, as with dnaK or dnaJ mutants, a secB null strain exhibits a strong cold-sensitive (Cs) phenotype. Through suppressor analyses, we found that inactivating mutations in the tig gene encoding TF fully relieve both the Cs phenotype and protein aggregation observed in the absence of SecB. This antagonistic effect of TF depends on its ribosome-binding and chaperone activities but unrelated to its peptidyl-prolyl cis/trans isomerase (PPIase) activity. Furthermore, in contrast to the previously known synergistic action of TF and DnaK/DnaJ above 30 degrees C, a tig null mutation partially suppresses the Cs phenotype exhibited by a compromised DnaK/DnaJ chaperone machine. The antagonistic role of TF is further exemplified by the fact that the secB dnaJ double mutant is viable only in the absence of TF. Finally, we show that, in the absence of TF, more SecA and ribosomes are associated with the inner membrane, suggesting that the presence of TF directly or indirectly interferes with the process of cotranslational protein targeting to the Sec translocon.
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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.