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

Conserved proline residues in the coiled coil-OB domain linkers of Rpt proteins facilitate eukaryotic proteasome base assembly.

The Journal of biological chemistry - 1 Jan 2000

Cheng Chin Leng, Wong Michael K, Li Yanjie, Hochstrasser Mark

Abstract excerpt

The proteasome is a large protease complex that degrades many different cellular proteins. In eukaryotes, the 26S proteasome contains six different subunits of the ATPases associated with diverse cellular activities family, Rpt1-Rpt6, which form a hexameric ring as part of the base subcomplex that drives unfolding and translocation of substrates into the proteasome core. Archaeal proteasomes contain only a single...

Read the complete abstract on PubMed

Topics

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

Share to Heat-Shock Proteins
Share to Proline

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Proteasome Endopeptidase Complex

Share to Protein Domains

Share to Repressor Proteins

Share to Saccharomyces cerevisiae Proteins

Share to Sequence Homology

Share to Ubiquitin-Protein Ligases

Source

Open in PubMed Open full text

Identifiers

PMID: 33862083
DOI: 10.1016/j.jbc.2021.100660
PMCID: PMC8134078

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Conserved proline residues in the coiled coil-OB domain linkers of Rpt proteins facilitate eukaryotic proteasome base assembly.PMID 33862083Read ↗

Structural defects in the regulatory particle-core particle interface of the proteasome induce a novel proteasome stress response.Semantic proximity Read ↗

An Inducible Chaperone Adapts Proteasome Assembly to StressSemantic proximity Read ↗

Proteasome beta-type subunits: unequal roles of propeptides in core particle maturation and a hierarchy of active site function.Semantic proximity Read ↗

Heterohexameric ring arrangement of the eukaryotic proteasomal ATPases: implications for proteasome structure and assembly.Semantic proximity Read ↗

Base-CP proteasome can serve as a platform for stepwise lid formation.Semantic proximity Read ↗

The C terminus of Rpt3, an ATPase subunit of PA700 (19 S) regulatory complex, is essential for 26 S proteasome assembly but not for activation.Semantic proximity Read ↗

The importance of proteasome grip depends on substrate stability.Semantic proximity Read ↗

Species-specific protein-protein interactions govern the humanization of the 20S proteasome in yeastSemantic proximity Read ↗

Interaction with the Assembly Chaperone Ump1 Promotes Incorporation of the β7 Subunit into Half-Proteasome Precursor Complexes Driving Their Dimerization.Semantic proximity Read ↗

The active sites of the eukaryotic 20 S proteasome and their involvement in subunit precursor processing.Semantic proximity Read ↗

Proteasome subunit α1 overexpression preferentially drives canonical proteasome biogenesis and enhances stress tolerance in yeastSemantic proximity Read ↗

Structural basis of human 20S proteasome biogenesisSemantic proximity Read ↗

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