ArticleThe Journal of biological chemistry2010
Versatility of trigger factor interactions with ribosome-nascent chain complexes.
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 22 papers.
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Who cites it
22 citing papers in PubMed.
- Quasi-continuous cotranslational compaction and folding of a multidomain protein.Nature communications · 2026Article
- Multivalent Interactions between Chaperone and Ribosome-Nascent Chain Complex Revealed by High-Speed AFM and MD Simulations.ACS nano · 2025Article
- Mechanistic Insights into Protein Biogenesis and Maturation on the Ribosome.Journal of molecular biology · 2025Review
- Trigger factor accelerates nascent chain compaction and folding.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Thermodynamic profiles for cotranslational trigger factor substrate recognition.Science advances · 2024Article
- Redox Brake Regulator RedB and FnrL Function as Yin-Yang Regulators of Anaerobic-Aerobic Metabolism in Rhodobacter capsulatus.Microbiology spectrum · 2022Article
- Protein folding in vitro and in the cell: From a solitary journey to a team effort.Biophysical chemistry · 2022Review
- Application of fluorescence correlation spectroscopy to investigate the dynamics of a ribosome-associated trigger factor inFrontiers in molecular biosciences · 2022Article
- Mechanisms of Cotranslational Protein Maturation in Bacteria.Frontiers in molecular biosciences · 2021Review
- The luminal domain of the ER stress sensor protein PERK binds misfolded proteins and thereby triggers PERK oligomerization.The Journal of biological chemistry · 2018Article
- Repair or destruction-an intimate liaison between ubiquitin ligases and molecular chaperones in proteostasis.FEBS letters · 2017Review
- Rotational restriction of nascent peptides as an essential element of co-translational protein folding: possible molecular players and structural consequences.Biology direct · 2017Article
- The ER stress sensor PERK luminal domain functions as a molecular chaperone to interact with misfolded proteins.Acta crystallographica. Section D, Structural biology · 2016Article
- Structural characterization of the interaction of α-synuclein nascent chains with the ribosomal surface and trigger factor.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The Trigger Factor Chaperone Encapsulates and Stabilizes Partial Folds of Substrate Proteins.PLoS computational biology · 2015Article
- Microbial peptidyl-prolyl cis/trans isomerases (PPIases): virulence factors and potential alternative drug targets.Microbiology and molecular biology reviews : MMBR · 2014Review
- Structural basis for protein antiaggregation activity of the trigger factor chaperone.Science (New York, N.Y.) · 2014Article
- Flexibility of the bacterial chaperone trigger factor in microsecond-timescale molecular dynamics simulations.Biophysical journal · 2013Article
- Article
- Translation elongation regulates substrate selection by the signal recognition particle.The Journal of biological chemistry · 2012Article
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Authors and funding
5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Trigger factor (TF) is the first molecular chaperone that interacts with nascent chains emerging from bacterial ribosomes. TF is a modular protein, consisting of an N-terminal ribosome binding domain, a PPIase domain, and a C-terminal domain, all of which participate in polypeptide binding. To directly monitor the interactions of TF with nascent polypeptide chains, TF variants were site-specifically labeled with an environmentally sensitive NBD fluorophore. We found a marked increase in TF-NBD fluorescence during translation of firefly luciferase (Luc) chains, which expose substantial regions of hydrophobicity, but not with nascent chains lacking extensive hydrophobic segments. TF remained associated with Luc nascent chains for 111 +/- 7 s, much longer than it remained bound to the ribosomes (t((1/2)) approximately 10-14 s). Thus, multiple TF molecules can bind per nascent chain during translation. The Escherichia coli cytosolic proteome was classified into predicted weak and strong interactors for TF, based on the occurrence of continuous hydrophobic segments in the primary sequence. The residence time of TF on the nascent chain generally correlated with the presence of hydrophobic regions and the capacity of nascent chains to bury hydrophobicity. Interestingly, TF bound the signal sequence of a secretory protein, pOmpA, but not the hydrophobic signal anchor sequence of the inner membrane protein FtsQ. On the other hand, proteins lacking linear hydrophobic segments also recruited TF, suggesting that TF can recognize hydrophobic surface features discontinuous in sequence. Moreover, TF retained significant affinity for the folded domain of the positively charged, ribosomal protein S7, indicative of an alternative mode of TF action. Thus, unlike other chaperones, TF appears to employ multiple mechanisms to interact with a wide range of substrate proteins.
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