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• W2190222425 endingPage "2003" @default.
• W2190222425 startingPage "1991" @default.
• W2190222425 abstract "Eukaryotic 20S proteasome assembly remains poorly understood. The subunits stack into four heteroheptameric rings; three inner-ring subunits (β1, β2, and β5) bear the protease catalytic residues and are synthesized with N-terminal propeptides. These propeptides are removed autocatalytically late in assembly. In Saccharomyces cerevisiae, β5 (Doa3/Pre2) has a 75-residue propeptide, β5pro, that is essential for proteasome assembly and can work in trans. We show that deletion of the poorly conserved N-terminal half of the β5 propeptide nonetheless causes substantial defects in proteasome maturation. Sequences closer to the cleavage site have critical but redundant roles in both assembly and self-cleavage. A conserved histidine two residues upstream of the autocleavage site strongly promotes processing. Surprisingly, although β5pro is functionally linked to the Ump1 assembly factor, trans-expressed β5pro associates only weakly with Ump1-containing precursors. Several genes were identified as dosage suppressors of trans-expressed β5pro mutants; the strongest encoded the β7 proteasome subunit. Previous data suggested that β7 and β5pro have overlapping roles in bringing together two half-proteasomes, but the timing of β7 addition relative to half-mer joining was unclear. Here we report conditions where dimerization lags behind β7 incorporation into the half-mer. Our results suggest that β7 insertion precedes half-mer dimerization, and the β7 tail and β5 propeptide have unequal roles in half-mer joining." @default.
• W2190222425 created "2016-06-24" @default.
• W2190222425 creator A5032098391 @default.
• W2190222425 creator A5037942759 @default.
• W2190222425 creator A5054066426 @default.
• W2190222425 creator A5079738340 @default.
• W2190222425 date "2016-01-01" @default.
• W2190222425 modified "2023-10-12" @default.
• W2190222425 title "Distinct Elements in the Proteasomal β5 Subunit Propeptide Required for Autocatalytic Processing and Proteasome Assembly" @default.
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• W2190222425 doi "https://doi.org/10.1074/jbc.m115.677047" @default.
• W2190222425 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4722473" @default.
• W2190222425 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26627836" @default.
• W2190222425 hasPublicationYear "2016" @default.
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