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Article

Functional dissection of Escherichia coli trigger factor: unraveling the function of individual domains.

Journal of bacteriology - 1 Jun 2004

Kramer G, Rutkowska A, Wegrzyn R D, Patzelt H, Kurz T A, Merz F, Rauch T, Vorderwülbecke S, Deuerling E, Bukau B

Abstract excerpt

In Escherichia coli, the ribosome-associated chaperone Trigger Factor (TF) promotes the folding of newly synthesized cytosolic proteins. TF is composed of three domains: an N-terminal domain (N), which mediates ribosome binding; a central domain (P), which has peptidyl-prolyl cis/trans isomerase activity and is involved in substrate binding in vitro; and a C-terminal domain (C) with unknown function. We...

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Identifiers

PMID: 15175291
DOI: 10.1128/JB.186.12.3777-3784.2004
PMCID: PMC419933

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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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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Functional dissection of Escherichia coli trigger factor: unraveling the function of individual domains.PMID 15175291Read ↗

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

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

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

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

Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli.Semantic proximity Read ↗

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

L23 protein functions as a chaperone docking site on the ribosome.Semantic proximity Read ↗

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

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

Trigger factor depletion or overproduction causes defective cell division but does not block protein export.Semantic proximity Read ↗

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

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