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Article

PPIase domain of trigger factor acts as auxiliary chaperone site to assist the folding of protein substrates bound to the crevice of trigger factor.

The international journal of biochemistry & cell biology - 1 Jun 2010

Liu Chuan-Peng, Zhou Qi-Ming, Fan Dong-Jie, Zhou Jun-Mei

Abstract excerpt

Trigger factor (TF) is the first chaperone encountered by nascent chains in bacteria, which consists of two modules: peptidyl-prolyl-cis/trans-isomerase (PPIase) domain and a crevice built by both N- and C-terminal domains. While the crevice is suggested to provide a protective space over the peptide exit site of ribosome for nascent polypeptides to fold, it remains unclear whether PPIase domain is directly...

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Identifiers

PMID: 20096367
DOI: 10.1016/j.biocel.2010.01.019

Genes

GAPDH

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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PPIase domain of trigger factor acts as auxiliary chaperone site to assist the folding of protein substrates bound to the crevice of trigger factor.PMID 20096367Read ↗

Structure and function of the molecular chaperone Trigger Factor.Semantic proximity Read ↗

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Identification of nascent chain interaction sites on trigger factor.Semantic proximity Read ↗

Functional dissection of Escherichia coli trigger factor: unraveling the function of individual domains.Semantic proximity Read ↗

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Comparative analysis of the molecular mechanism of heat shock proteins from pathogenic and non-pathogenic <i>E.coli</i>Semantic proximity Read ↗

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Identification of Substrates of Cytoplasmic Peptidyl-Prolyl Cis/Trans Isomerases and Their Collective Essentiality in Escherichia Coli.Semantic proximity Read ↗

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