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

Successive action of Escherichia coli chaperones in vivo.

Molecular microbiology - 1 Dec 1994

Gaitanaris G A, Vysokanov A, Hung S C, Gottesman M E, Gragerov A

Abstract excerpt

Escherichia coli DnaK, DnaJ and GrpE are required for renaturation of heat-inactivated lambda Cl857 repressor (Gaitanaris et al., 1990). Here we demonstrate that in addition to the above three proteins, GroEL and GroES are necessary for the Cl857 repressor to acquire full activity at the permissive temperature. Although full-length soluble repressor is present at normal amounts, the protein has reduced specific...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to DNA-Binding Proteins
Share to Escherichia coli

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Escherichia coli Proteins

Share to Mutation

Share to Protein Biosynthesis

Share to Protein Conformation

Share to Repressor Proteins

Source

Identifiers

PMID: 7715448
DOI: 10.1111/j.1365-2958.1994.tb01322.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Successive action of Escherichia coli chaperones in vivo.PMID 7715448Read ↗

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

DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli.Semantic proximity Read ↗

The 70-kDa heat-shock protein/DnaK chaperone system is required for the productive folding of ribulose-biphosphate carboxylase subunits in Escherichia coli.Semantic proximity Read ↗

The chaperonin GroEL and other heat-shock proteins, besides DnaK, participate in ribosome biogenesis in Escherichia coli.Semantic proximity Read ↗

Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli.Semantic proximity Read ↗

Functional defects of the DnaK756 mutant chaperone of Escherichia coli indicate distinct roles for amino- and carboxyl-terminal residues in substrate and co-chaperone interaction and interdomain communication.Semantic proximity Read ↗

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

DnaK-dependent ribosome biogenesis in Escherichia coli: competition for dominance between the alleles dnaK756 and dnaK+.Semantic proximity Read ↗

Protein folding in the cytoplasm of Escherichia coli: requirements for the DnaK-DnaJ-GrpE and GroEL-GroES molecular chaperone machines.Semantic proximity Read ↗

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

Physiological roles of the DnaK and GroE stress proteins: catalysts of protein folding or macromolecular sponges?Semantic proximity Read ↗

GroES/GroEL and DnaK/DnaJ have distinct roles in stress responses and during cell cycle progression in Caulobacter crescentus.Semantic proximity Read ↗

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