Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

FEBS letters - 20 Aug 2010

Gupta Rashmi, Lakshmipathy Sathish Kumar, Chang Hung-Chun, Etchells Stephanie A, Hartl F Ulrich

Abstract excerpt

Recombinant expression of eukaryotic proteins in bacteria often results in misfolding and aggregation. The ribosome-binding Trigger factor (TF) is the first molecular chaperone that interacts with nascent polypeptide chains in bacteria. Here we show that mutant TF lacking the PPIase domain (TFNC)...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Escherichia coli Proteins
Share to Luciferases, Firefly
Share to Molecular Chaperones

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Peptidylprolyl Isomerase

Share to Protein Biosynthesis

Share to Protein Folding

Share to ras Proteins

Share to Tetrahydrofolate Dehydrogenase

Source

Identifiers

PMID: 20659464
DOI: 10.1016/j.febslet.2010.07.036

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20659464-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Trigger factor lacking the PPIase domain can enhance the folding of eukaryotic multi-domain proteins in Escherichia coli.PMID 20659464Read ↗

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

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 ↗

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 ↗

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

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

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

Slowing bacterial translation speed enhances eukaryotic protein folding efficiency.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 ↗

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

Trigger Factor-Mediated Prolyl Isomerization Influences Maturation of the Streptococcus pyogenes Cysteine ProteaseSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.