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Article

The chaperone activity of trigger factor is distinct from its isomerase activity during co-expression with adenylate kinase in Escherichia coli.

FEBS letters - 5 Oct 2001

Li Z Y, Liu C P, Zhu L Q, Jing G Z, Zhou J M

Abstract excerpt

To investigate the molecular chaperone function of trigger factor (TF) and its relationship with isomerase activity in vivo, the assisted folding of adenylate kinase (AK) by TF in Escherichia coli was examined by measuring the amounts of soluble AK produced during co-expression. When the mutant of chicken AK, P17G, is expressed in plasmid pBVAK, 95% of the protein is found in inclusion bodies. Co-expression of AK...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 11591381
DOI: 10.1016/s0014-5793(01)02896-4

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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The chaperone activity of trigger factor is distinct from its isomerase activity during co-expression with adenylate kinase in Escherichia coli.PMID 11591381Read ↗

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

Trigger factor and DnaK cooperate in folding of newly synthesized proteins.Semantic proximity Read ↗

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

Evaluation of similarities in the cis/trans isomerase function of trigger factor and DnaK.Semantic proximity Read ↗

Trigger factor lacking the PPIase domain can enhance the folding of eukaryotic multi-domain proteins in Escherichia coli.Semantic proximity Read ↗

The C-terminal domain of Escherichia coli trigger factor represents the central module of its chaperone activity.Semantic proximity Read ↗

Structural rearrangements and the unfolding mechanism of a Trigger Factor mutant studied by multiple structural probes.Semantic proximity Read ↗

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

Interaction of trigger factor with the ribosome.Semantic proximity Read ↗

Cyclophilin and Trigger Factor from <i>Bacillus </i><i>s</i><i>ubtilis</i> Catalyze in Vitro Protein Folding and Are Necessary for Viability under Starvation ConditionsSemantic proximity Read ↗

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

Trigger Factor can antagonize both SecB and DnaK/DnaJ chaperone functions in Escherichia coli.Semantic proximity Read ↗

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