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

Functional analysis of Rpn6p, a lid component of the 26 S proteasome, using temperature-sensitive rpn6 mutants of the yeast Saccharomyces cerevisiae.

The Journal of biological chemistry - 25 Feb 2005

Isono Erika, Saito Naoko, Kamata Naoko, Saeki Yasushi, Toh-E Akio

Abstract excerpt

Rpn6p is a component of the lid of the 26 S proteasome. We isolated and analyzed two temperature-sensitive rpn6 mutants in the yeast, Saccharomyces cerevisiae. Both mutants showed defects in protein degradation in vivo. However, the affinity-purified 26 S proteasome of the rpn6 mutants grown at the permissive temperature degraded polyubiquitinated Sic1p efficiently, even at a higher temperature. Interestingly,...

Read the complete abstract on PubMed

Topics

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

Share to Cell Cycle Proteins
Share to Endopeptidases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Proteasome Endopeptidase Complex

Share to Repressor Proteins

Share to Saccharomyces cerevisiae

Share to Saccharomyces cerevisiae Proteins

Share to Temperature

Share to Ubiquitin

Source

Identifiers

PMID: 15611133
DOI: 10.1074/jbc.M409364200

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

Functional analysis of Rpn6p, a lid component of the 26 S proteasome, using temperature-sensitive rpn6 mutants of the yeast Saccharomyces cerevisiae.PMID 15611133Read ↗

Rpn6p, a proteasome subunit from Saccharomyces cerevisiae, is essential for the assembly and activity of the 26 S proteasome.Semantic proximity Read ↗

Integrity of the Saccharomyces cerevisiae Rpn11 protein is critical for formation of proteasome storage granules (PSG) and survival in stationary phase.Semantic proximity Read ↗

Sem1p is a novel subunit of the 26 S proteasome from Saccharomyces cerevisiae.Semantic proximity Read ↗

Chaperone-mediated pathway of proteasome regulatory particle assembly.Semantic proximity Read ↗

Disruption of Rpn4-Induced Proteasome Expression in Saccharomyces cerevisiae Reduces Cell Viability Under Stressed ConditionsSemantic proximity Read ↗

Rpn5 is a conserved proteasome subunit and required for proper proteasome localization and assembly.Semantic proximity Read ↗

N-Myristoylation of the Rpt2 subunit of the yeast 26S proteasome is implicated in the subcellular compartment-specific protein quality control system.Semantic proximity Read ↗

The Cdc6 protein is ubiquitinated in vivo for proteolysis in Saccharomyces cerevisiae.Semantic proximity Read ↗

Crystal structure of yeast rpn14, a chaperone of the 19 S regulatory particle of the proteasome.Semantic proximity Read ↗

Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase.Semantic proximity Read ↗

N-Terminal methylation of proteasome subunit Rpt1 in yeast.Semantic proximity Read ↗

Genetic dissection of the yeast 26S proteasome: cell cycle defects caused by the Deltarpn9 mutation.Semantic proximity Read ↗

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