Proteasome activation by REG molecules lacking homolog-specific inserts.

The Journal of Biological Chemistry
Z ZhangMartin Rechsteiner

Abstract

The peptidase activities of eukaryotic proteasomes are markedly activated by the 11 S REG or PA28. The three identified REG subunits, designated alpha, beta, and gamma, differ significantly in sequence over a short span of 15-30 amino acids that we call homolog-specific inserts. These inserts were deleted from each REG to produce the mutant proteins REGalphaDeltai, REGbetaDeltai, and REGgammaDeltai. The purified recombinant proteins were then tested for their ability to oligomerize and activate the proteasome. Both REGalphaDeltai and REGgammaDeltai formed apparent heptamers and activated human red cell proteasomes to the same extent as their full-length counterparts. By contrast, REGbetaDeltai exhibited, at low protein concentrations, reduced proteasome activation when compared with the wild-type REGbeta protein. REGbetaDeltai was able to form hetero-oligomers with a single site, monomeric REGalpha mutant and with REGalphaDeltai. At low concentrations, the REGalphaDeltai/REGbetaDeltai hetero-oligomers stimulated the proteasome less than REGalpha/REGbeta oligomers formed from wild-type subunits, and the reduced activation by REGalphaDeltai/REGbetaDeltai was due to removal of the REGbeta insert, not the REGalpha insert. These stu...Continue Reading

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Citations

Apr 11, 2001·Biochimie·J Li, M Rechsteiner
Dec 22, 1999·The Biochemical Journal·M RechsteinerV Ustrell
Jun 29, 2000·Annual Review of Biochemistry·D VogesW Baumeister
Feb 5, 2013·Biochemical and Biophysical Research Communications·Masaaki SugiyamaKoichi Kato
Apr 28, 2004·Archives of Biochemistry and Biophysics·Xiaolin GaoMartin Rechsteiner
Feb 11, 2021·Biomolecules·Paolo Cascio

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