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 language | English |
|---|---|
| Pages (from-to) | 397-401 |
| Number of pages | 5 |
| Journal | Archives of Biochemistry and Biophysics |
| Volume | 349 |
| Issue number | 2 |
| DOIs | |
| State | Published - Jan 15 1998 |
| Externally published | Yes |
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Keywords
- Proteasome
- Protein kinase CK2
- Protein phosphorylation
- Protein turnover
- Saccharomyces cerevisiae
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
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. / Pardo, Patricia S.; Murray, Pedro Fernández; Walz, Katherina; Franco, Lorena; Passeron, Susana.
In: Archives of Biochemistry and Biophysics, Vol. 349, No. 2, 15.01.1998, p. 397-401.Research output: Contribution to journal › Article
}
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
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
UR - http://www.scopus.com/inward/record.url?scp=0032518167&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032518167&partnerID=8YFLogxK
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 -