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Literature summary for 5.6.1.5 extracted from

  • Inobe, T.; Genmei, R.
    N-Terminal coiled-coil structure of ATPase subunits of 26S proteasome is crucial for proteasome function (2015), PLoS ONE, 10, e0134056.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.1.5

Cloned(Commentary)

Cloned (Comment) Organism
Mouse Rpt2 rescued the expression of yeast Rpt2 with a weak growth defect Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
additional information conditional knockdown yeast strains for each Rpt subunit. Since all Rpt subunits are lethal to almost all species, including yeast and higher species, rescue experiments using individual Rpt subunits in conditional knockdown strains for each Rpt subunit are conducted to analyze the functional compensation of exogenic mutant Rpt subunits in cells in which the expression of endogenous Rpt subunits is conditionally suppressed. Mouse Rpt subunits can be substituted for yeast Rpt subunits Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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Subunits

Subunits Comment Organism
More heterohexameric Rpt ring Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
Rpt subunit
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 Saccharomyces cerevisiae

General Information

General Information Comment Organism
malfunction destabilization of the N-terminal coiled-coil regions of Rpt subunits causes proteasome defects, destabilization of Rpt subunits hampers yeast growth Saccharomyces cerevisiae
additional information the heterohexameric AAA+ ATPase Rpt subunits play a central role in proteasome activity by the engagement of substrate unfolding and translocation for degradation, the N-terminal coiled-coil structure of the ATPase subunits of the 26S proteasome is crucial for proteasome function. In contrast to AAA+ ATPase domains, their N-terminal regions of Rpt subunits substantially differ from each other. The primary role of coiled-coil structure is the maintenance of the ring structure with the defined order, the coiled-coil region is also be involved in substrate recognition and an interaction between lid and base subcomplexes. The base subcomplex mainly consists of a ring of six distinct AAA+ ATPase subunits designated Rpt1-6, which share highly homologous AAA+ ATPase domains, while ATPase activity and substrate-binding affinity of each Rpt subunit significantly differ from each other Saccharomyces cerevisiae