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   Articles with "trigger factor" as a keyword



Global Analysis of the Impact of Deleting Trigger Factor on the Transcriptome Profile of Escherichia coli

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recommendations! Published in 2017 at "Journal of Cellular Biochemistry"

DOI: 10.1002/jcb.25620

Abstract: Trigger factor (TF) is a key component of prokaryotic chaperone network, which is involved various basic cellular processes such as nascent peptide folding, protein trafficking, ribosome assembly. To better understanding the physiological roles of TF,… read more here.

Keywords: escherichia coli; profile; transcriptome profile; trigger factor ... See more keywords

Investigation of the probable trigger factor for large landslides in north of Dehdasht, Iran

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recommendations! Published in 2020 at "Natural Hazards"

DOI: 10.1007/s11069-020-04382-1

Abstract: Charosa and Dehdasht is a part of folded Zagros that is located in the Kohgiluyeh and Boyer-Ahmad Province in southwestern Iran. This area is covered with several Zagros anticlines such as the Kuh-e-Sefid, Sartal, Nil,… read more here.

Keywords: landslides north; factor large; trigger factor; probable trigger ... See more keywords

Trigger factor chaperone acts as a mechanical foldase

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recommendations! Published in 2017 at "Nature Communications"

DOI: 10.1038/s41467-017-00771-6

Abstract: Proteins fold under mechanical forces in a number of biological processes, ranging from muscle contraction to co-translational folding. As force hinders the folding transition, chaperones must play a role in this scenario, although their influence… read more here.

Keywords: factor; chaperone; folding force; trigger factor ... See more keywords

The dynamic dimer structure of the chaperone Trigger Factor

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recommendations! Published in 2017 at "Nature Communications"

DOI: 10.1038/s41467-017-02196-7

Abstract: The chaperone Trigger Factor (TF) from Escherichia coli forms a dimer at cellular concentrations. While the monomer structure of TF is well known, the spatial arrangement of this dimeric chaperone storage form has remained unclear.… read more here.

Keywords: trigger factor; dimer; chaperone trigger; dimer structure ... See more keywords

A truncated variant of the ribosome-associated trigger factor specifically contributes to plant chloroplast ribosome biogenesis

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recommendations! Published in 2025 at "Nature Communications"

DOI: 10.1038/s41467-025-55813-1

Abstract: Molecular chaperones are essential throughout a protein’s life and act already during protein synthesis. Bacteria and chloroplasts of plant cells share the ribosome-associated chaperone trigger factor (Tig1 in plastids), facilitating maturation of emerging nascent polypeptides.… read more here.

Keywords: plant; ribosome associated; ribosome biogenesis; trigger factor ... See more keywords

Dynamic binding of the bacterial chaperone Trigger factor to translating ribosomes in Escherichia coli

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recommendations! Published in 2024 at "Proceedings of the National Academy of Sciences of the United States of America"

DOI: 10.1101/2024.03.27.586930

Abstract: The bacterial chaperone Trigger factor (TF) binds to ribosome-nascent chain complexes (RNCs) and co-translationally aids the folding of proteins in bacteria. Decades of studies have given a broad, but often conflicting, description of the substrate… read more here.

Keywords: escherichia coli; trigger factor; rnc binding; bacterial chaperone ... See more keywords

Bacillus subtilis forms twisted cells with cell wall integrity defects upon removal of the molecular chaperones DnaK and trigger factor

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recommendations! Published in 2023 at "Frontiers in Microbiology"

DOI: 10.3389/fmicb.2022.988768

Abstract: The protein homeostasis network ensures a proper balance between synthesis, folding, and degradation of all cellular proteins. DnaK and trigger factor (TF) are ubiquitous bacterial molecular chaperones that assist in protein folding, as well as… read more here.

Keywords: molecular chaperones; cell wall; dnak trigger; wall integrity ... See more keywords

Application of fluorescence correlation spectroscopy to investigate the dynamics of a ribosome-associated trigger factor in Escherichia coli

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recommendations! Published in 2022 at "Frontiers in Molecular Biosciences"

DOI: 10.3389/fmolb.2022.891128

Abstract: Co-translational protein folding is one of the central topics in molecular biology. In Escherichia coli, trigger factor (TF) is a primary chaperone that facilitates co-translational folding by directly interacting with nascent polypeptide chains on translating… read more here.

Keywords: investigate; escherichia coli; spectroscopy; fluorescence correlation ... See more keywords