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

A Mutant Chaperonin That Is Functional at Lower Temperatures Enables Hyperthermophilic Archaea To Grow under Cold-Stress Conditions.

Journal of bacteriology - 1 Aug 2015

Gao Le, Imanaka Tadayuki, Fujiwara Shinsuke

Abstract excerpt

UNLABELLED: Thermococcus kodakarensis grows optimally at 85°C and possesses two chaperonins, cold-inducible CpkA and heat-inducible CpkB, which are involved in adaptation to low and high temperatures, respectively. The two chaperonins share a high sequence identity (77%), except in their C-terminal regions. CpkA, which contains tandem repeats of a GGM motif, shows its highest ATPase activity at 60°C to 70°C,...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphatases
Share to Archaeal Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cold Temperature

Share to DNA, Archaeal

Share to Hot Temperature

Share to Molecular Chaperones

Share to Plasmids

Share to Sequence Alignment

Source

Open in PubMed Open full text

Identifiers

PMID: 26013483
DOI: 10.1128/JB.00279-15
PMCID: PMC4507335

Provenance

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

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A Mutant Chaperonin That Is Functional at Lower Temperatures Enables Hyperthermophilic Archaea To Grow under Cold-Stress Conditions.PMID 26013483Read ↗

Isolation and characterization of a second subunit of molecular chaperonin from Pyrococcus kodakaraensis KOD1: analysis of an ATPase-deficient mutant enzyme.Semantic proximity Read ↗

Archaeal RNA polymerase subunits E and F are not required for transcription in vitro, but a Thermococcus kodakarensis mutant lacking subunit F is temperature-sensitive.Semantic proximity Read ↗

Mutation design of a thermophilic Rubisco based on three-dimensional structure enhances its activity at ambient temperature.Semantic proximity Read ↗

Phosphoenolpyruvate synthase plays an essential role for glycolysis in the modified Embden-Meyerhof pathway in Thermococcus kodakarensis.Semantic proximity Read ↗

A novel scoring function for discriminating hyperthermophilic and mesophilic proteins with application to predicting relative thermostability of protein mutants.Semantic proximity Read ↗

A modulator domain controlling thermal stability in the Group II chaperonins of Archaea.Semantic proximity Read ↗

Mutation of the gene encoding the ribonuclease P RNA in the hyperthermophilic archaeon Thermococcus kodakarensis causes decreased growth rate and impaired processing of tRNA precursors.Semantic proximity Read ↗

Analysis of the temperature-sensitive mutation of Escherichia coli pantothenate kinase reveals YbjN as a possible protein stabilizer.Semantic proximity Read ↗

Examine the Correlation between Heat Shock Protein IbpA and Heat Tolerance in Cronobacter sakazakii.Semantic proximity Read ↗

An ornithine ω-aminotransferase required for growth in the absence of exogenous proline in the archaeon Thermococcus kodakarensis.Semantic proximity Read ↗

Substitutions of coenzyme-binding, nonpolar residues improve the low-temperature activity of thermophilic dehydrogenases.Semantic proximity Read ↗

The stability of the coiled-coil structure near to N-terminus influence the heat resistance of harpin proteins from Xanthomonas.Semantic proximity Read ↗

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