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Article

L23 protein functions as a chaperone docking site on the ribosome.

Nature - 12 Sept 2002

Kramer Günter, Rauch Thomas, Rist Wolfgang, Vorderwülbecke Sonja, Patzelt Holger, Schulze-Specking Agnes, Ban Nenad, Deuerling Elke, Bukau Bernd

Abstract excerpt

During translation, the first encounter of nascent polypeptides is with the ribosome-associated chaperones that assist the folding process--a principle that seems to be conserved in evolution. In Escherichia coli, the ribosome-bound Trigger Factor chaperones the folding of cytosolic proteins by interacting with nascent polypeptides. Here we identify a ribosome-binding motif in the amino-terminal domain of Trigger...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 12226666
DOI: 10.1038/nature01047

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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

L23 protein functions as a chaperone docking site on the ribosome.PMID 12226666Read ↗

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

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

A functional connection between translation elongation and protein folding at the ribosome exit tunnel in Saccharomyces cerevisiae.Semantic proximity Read ↗

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

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

SecA interacts with ribosomes in order to facilitate posttranslational translocation in bacteria.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 ↗

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

Trigger factor is a bona fide secretory pathway chaperone that interacts with SecB and the translocaseSemantic proximity Read ↗

An intrinsically disordered nascent protein interacts with specific regions of the ribosomal surface near the exit tunnel.Semantic proximity Read ↗

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

A conserved motif is prerequisite for the interaction of NAC with ribosomal protein L23 and nascent chains.Semantic proximity Read ↗

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