ArticleMolecular microbiology2016
Single-molecule dynamics of the molecular chaperone trigger factor in living cells.
Article in Molecular microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
13 citing papers in PubMed, 19 citations in OpenAlex.
- Multivalent weak contacts shape chaperone-nascent protein interactions.bioRxiv : the preprint server for biology · 2026Article
- Analysis of Complex Single-Molecule Kinetics: A Protocol for Single-Molecule Interaction Simulations (SMIS).Methods in molecular biology (Clifton, N.J.) · 2026Article
- Multivalent Interactions between Chaperone and Ribosome-Nascent Chain Complex Revealed by High-Speed AFM and MD Simulations.ACS nano · 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
- Thermodynamic profiles for cotranslational trigger factor substrate recognition.Science advances · 2024Article
- Metabolic and Oxidative Stress Effects on the Spectroelectrochemical Behavior of SingleChemical & biomedical imaging · 2023Article
- Critical Beginnings: Selective Tuning of Solubility and Structural Accuracy of Newly Synthesized Proteins by the Hsp70 Chaperone System.The journal of physical chemistry. B · 2023Article
- Real-time single-molecule 3D tracking in E. coli based on cross-entropy minimization.Nature communications · 2023Article
- Application of fluorescence correlation spectroscopy to investigate the dynamics of a ribosome-associated trigger factor inFrontiers in molecular biosciences · 2022Article
- Article
- Streptococcus pneumoniae Cell Wall-Localized Trigger Factor Elicits a Protective Immune Response and Contributes to Bacterial Adhesion to the Host.Scientific reports · 2019Article
- ColiCoords: A Python package for the analysis of bacterial fluorescence microscopy data.PloS one · 2019Article
- SMTracker: a tool for quantitative analysis, exploration and visualization of single-molecule tracking data reveals highly dynamic binding of B. subtilis global repressor AbrB throughout the genome.Scientific reports · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
In bacteria, trigger factor (TF) is the molecular chaperone that interacts with the ribosome to assist the folding of nascent polypeptides. Studies in vitro have provided insights into the function and mechanism of TF. Much is to be elucidated, however, about how TF functions in vivo. Here, we use single-molecule tracking, in combination with genetic manipulations, to study the dynamics and function of TF in living E. coli cells. We find that TF, besides interacting with the 70S ribosome, may also bind to ribosomal subunits and form TF-polypeptide complexes that may include DnaK/DnaJ proteins. The TF-70S ribosome interactions are highly dynamic inside cells, with an average residence time of ∼0.2 s. Our results confirm that the signal recognition particle weakens TF's interaction with the 70S ribosome, and further identify that this weakening mainly results from a change in TF's binding to the 70S ribosome, rather than its unbinding. Moreover, using photoconvertible bimolecular fluorescence complementation, we selectively probe TF
Indexed as
Identifiers
What OpenQuestion holds
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.