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Article

Identification of nascent chain interaction sites on trigger factor.

The Journal of biological chemistry - 20 Apr 2007

Lakshmipathy Sathish K, Tomic Sladjana, Kaiser Christian M, Chang Hung-Chun, Genevaux Pierre, Georgopoulos Costa, Barral José M, Johnson Arthur E, Hartl F Ulrich, Etchells Stephanie A

Abstract excerpt

The role of ribosome-binding molecular chaperones in protein folding is not yet well understood. Trigger factor (TF) is the first chaperone to interact with nascent polypeptides as they emerge from the bacterial ribosome. It binds to the ribosome as a monomer but forms dimers in free solution. Based on recent crystal structures, TF has an elongated shape, with the peptidyl-prolyl-cis/trans-isomerase (PPIase)...

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Identifiers

PMID: 17296610
DOI: 10.1074/jbc.M609871200

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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.

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Identification of nascent chain interaction sites on trigger factor.PMID 17296610Read ↗

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

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

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

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