ArticleJournal of bacteriology2004
Functional dissection of Escherichia coli trigger factor: unraveling the function of individual domains.
Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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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.
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Who cites it
35 citing papers in PubMed, 89 citations in OpenAlex.
- Sec and Tat Mediated Secretion Safeguards Mycobacterium tuberculosis Membrane Homeostasis.Molecular & cellular proteomics : MCP · 2026Article
- Genome-Wide Analysis of Tea FK506-Binding Proteins (FKBPs) Reveals ThatInternational journal of molecular sciences · 2025Article
- A truncated variant of the ribosome-associated trigger factor specifically contributes to plant chloroplast ribosome biogenesis.Nature communications · 2025Article
- Dynamic binding of the bacterial chaperone Trigger factor to translating ribosomes inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- Protein folding in vitro and in the cell: From a solitary journey to a team effort.Biophysical chemistry · 2022Review
- A Review: Molecular Chaperone-mediated Folding, Unfolding and Disaggregation of Expressed Recombinant Proteins.Cell biochemistry and biophysics · 2021Review
- Trigger Factor in Association with the ClpP1P2 Heterocomplex ofACS omega · 2021Article
- Redefining Molecular Chaperones as Chaotropes.Frontiers in molecular biosciences · 2021Review
- Mechanisms of Cotranslational Protein Maturation in Bacteria.Frontiers in molecular biosciences · 2021Review
- How Quality Control Systems AID Sec-Dependent Protein Translocation.Frontiers in molecular biosciences · 2021Review
- The Role of Plastidic Trigger Factor Serving Protein Biogenesis in Green Algae and Land Plants.Plant physiology · 2019Article
- Article
- Rotational restriction of nascent peptides as an essential element of co-translational protein folding: possible molecular players and structural consequences.Biology direct · 2017Article
- Regulation by a chaperone improves substrate selectivity during cotranslational protein targeting.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins.Cellular and molecular life sciences : CMLS · 2014Review
- Structural basis for protein antiaggregation activity of the trigger factor chaperone.Science (New York, N.Y.) · 2014Article
- Hydrophobic collapse of trigger factor monomer in solution.PloS one · 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
- Transcriptomic profiling of the oyster pathogen Vibrio splendidus opens a window on the evolutionary dynamics of the small RNA repertoire in the Vibrio genus.RNA (New York, N.Y.) · 2012Article
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Escherichia coli, the ribosome-associated chaperone Trigger Factor (TF) promotes the folding of newly synthesized cytosolic proteins. TF is composed of three domains: an N-terminal domain (N), which mediates ribosome binding; a central domain (P), which has peptidyl-prolyl cis/trans isomerase activity and is involved in substrate binding in vitro; and a C-terminal domain (C) with unknown function. We investigated the contributions of individual domains (N, P, and C) or domain combinations (NP, PC, and NC) to the chaperone activity of TF in vivo and in vitro. All fragments comprising the N domain (N, NP, NC) complemented the synthetic lethality of Deltatig DeltadnaK in cells lacking TF and DnaK, prevented protein aggregation in these cells, and cross-linked to nascent polypeptides in vitro. However, DeltatigDeltadnaK cells expressing the N domain alone grew more slowly and showed less viability than DeltatigDeltadnaK cells synthesizing either NP, NC, or full-length TF, indicating beneficial contributions of the P and C domains to TF's chaperone activity. In an in vitro system with purified components, none of the TF fragments assisted the refolding of denatured d-glyceraldehyde-3-phosphate dehydrogenase in a manner comparable to that of wild-type TF, suggesting that the observed chaperone activity of TF fragments in vivo is dependent on their localization at the ribosome. These results indicate that the N domain, in addition to its function to promote binding to the ribosome, has a chaperone activity per se and is sufficient to substitute for TF in vivo.
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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.