In vivo and in vitro phosphorylation of the α7/PRS1 subunit of Saccharomyces cerevisiae 20 S proteasome: In vitro phosphorylation by protein kinase CK2 is absolutely dependent on polylysine

Patricia S. Pardo, Pedro Fernández Murray, Katherina Walz, Lorena Franco, Susana Passeron

Research output: Contribution to journalArticle

21 Scopus citations

Abstract

In this paper, we show that the Saccharomyces cerevisiae 20 S proteasome subunit 1 (PRS1), recently renamed as α7, is the main in vivo phosphorylated and in vitro CK2-phosphorylatable proteasome component. In vitro phosphorylation occurs only in the presence of polylysine, a characteristic that distinguishes the yeast proteasome from mammalian ones which are phosphorylated by CK2 in the absence of polylysine. A peptide reproducing the long acidic C-terminal tail of α7/PRS1, where consensus CK2 phosphorylation sites are located, was also phosphorylated by the CK2 holoenzyme in a polylysine-dependent manner, suggesting that this region contains structural features responsible for this particular behavior.

Original languageEnglish (US)
Pages (from-to)397-401
Number of pages5
JournalArchives of Biochemistry and Biophysics
Volume349
Issue number2
DOIs
StatePublished - Jan 15 1998
Externally publishedYes

Keywords

  • Proteasome
  • Protein kinase CK2
  • Protein phosphorylation
  • Protein turnover
  • Saccharomyces cerevisiae

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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