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- W2046972298 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." @default.
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- W2046972298 date "1998-01-01" @default.
- W2046972298 modified "2023-10-09" @default.
- W2046972298 title "In Vivoandin VitroPhosphorylation of the α7/PRS1 Subunit ofSaccharomyces cerevisiae20 S Proteasome:In VitroPhosphorylation by Protein Kinase CK2 Is Absolutely Dependent on Polylysine" @default.
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- W2046972298 doi "https://doi.org/10.1006/abbi.1997.0466" @default.
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