TY - JOUR
T1 - In vivo and in vitro phosphorylation of the α7/PRS1 subunit of Saccharomyces cerevisiae 20 S proteasome
T2 - In vitro phosphorylation by protein kinase CK2 is absolutely dependent on polylysine
AU - Pardo, Patricia S.
AU - Murray, Pedro Fernández
AU - Walz, Katherina
AU - Franco, Lorena
AU - Passeron, Susana
N1 - Funding Information:
We are grateful to Dr. Olaf-G. Issinger for his kind donation of rhCK2 enzymes and to Dr. Klaus Hendil his generous gift of the monoclonal antibody against human C8 subunit. We are also indebted to Dr. Wolfgang Hilt for providing us with the yBM 178 S. cerevisiae strain. This work was supported by grants from the Con-sejo Nacional de Investigaciones CientõBficas y TeÂcnicas (CONICET), Universidad de Buenos Aires and the International Centre for Genetic Engineering and Biotechnology (ICGEB). S.P. is a research member from the CONICET and K.W. is a research fellow from the same institution.
PY - 1998/1/15
Y1 - 1998/1/15
N2 - 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.
AB - 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.
KW - Proteasome
KW - Protein kinase CK2
KW - Protein phosphorylation
KW - Protein turnover
KW - Saccharomyces cerevisiae
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U2 - 10.1006/abbi.1997.0466
DO - 10.1006/abbi.1997.0466
M3 - Article
C2 - 9448731
AN - SCOPUS:0032518167
VL - 349
SP - 397
EP - 401
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
SN - 0003-9861
IS - 2
ER -