In vivo and in vitro phosphorylation of the alpha 7/PRS1 subunit of Saccharomyces cerevisiae 20 S proteasome: in vitro phosphorylation by protein kinase CK2 is absolutely dependent on polylysine

Archives of Biochemistry and Biophysics
P S PardoS Passeron

Abstract

In this paper, we show that the Saccharomyces cerevisiae 20 S proteasome subunit 1 (PRS1), recently renamed as alpha 7, 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 alpha 7/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.

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Citations

Jul 31, 2010·Archaea : an International Microbiological Journal·Matthew A HumbardJulie A Maupin-Furlow
Mar 5, 2017·Protein & Cell·Xing GuoMark J Chen
Feb 13, 2002·Electrophoresis·Yuko IwafuneHisashi Hirano
Mar 20, 2012·Cell and Tissue Research·Janetti SignorelliPatricio Morales
Mar 13, 2003·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Flavio Meggio, Lorenzo A Pinna
Sep 4, 2014·The Journal of Biological Chemistry·Geetha S HewawasamJennifer L Gerton
Mar 4, 2000·Archives of Biochemistry and Biophysics·P Fernández MurrayS Passeron
Jul 20, 2002·Archives of Biochemistry and Biophysics·Pedro Fernández MurraySusana Passeron

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