Protein kinases phosphorylating acidic ribosomal proteins from yeast cells
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, přehledy
PubMed
10588049
DOI
10.1007/bf02816233
Knihovny.cz E-zdroje
- MeSH
- fosforylace MeSH
- fungální proteiny metabolismus MeSH
- kaseinkinasa II MeSH
- protein-serin-threoninkinasy metabolismus MeSH
- proteinkinasy metabolismus MeSH
- ribozomální proteiny metabolismus MeSH
- Saccharomyces cerevisiae enzymologie MeSH
- Publikační typ
- časopisecké články MeSH
- přehledy MeSH
- Názvy látek
- 60S ribosomal protein kinase MeSH Prohlížeč
- fungální proteiny MeSH
- kaseinkinasa II MeSH
- protein-serin-threoninkinasy MeSH
- proteinkinasy MeSH
- RAP kinase MeSH Prohlížeč
- ribozomální proteiny MeSH
Phosphorylation of ribosomal acidic proteins of Saccharomyces cerevisiae is an important mechanism regulating a number of active ribosomes. The key role in the regulatory mechanism is played by specific phosphoprotein kinases and phosphoprotein phosphatases. Three different cAMP-independent protein kinases phosphorylating acidic ribosomal proteins have been identified and characterized. The protein kinase 60S (PK60S), RAP kinase, and casein kinase type 2 (CK2). All three protein kinases phosphorylate serine residues which are localized in the C-terminal end of phosphoproteins. Synthetic peptides were used to determinate the amino acid sequence of phosphoacceptor site for PK60S. Peptide AAEESDDD derived from phosphoproteins YP1 beta/beta' and YP2 alpha turned out to be the best substrate for PK60S. A number of halogenated benzimidazoles and 2-azabenzimidazoles were tested as inhibitors of the three protein kinases. 4,5,6,7-Tetrabromo-2-azabenzimidazole inhibits phosphorylation only of these polypeptides phosphorylated by protein kinase 60S, namely YP1 beta/beta' and YP2 alpha, but not the other, YP1 alpha and YP2 beta phosphorylated by protein kinases RAP and CK2. RAP kinase has been found in an active form in the soluble fraction of S. cerevisiae. The enzyme uses ATP as a phosphate donor and is less sensitive to heparin than casein kinase 2. RAP kinase monophosphorylates the four acidic proteins. The ribosome-bound proteins are a better substrate for the enzyme. Multifunctional CK2 kinase phosphorylate all four acidic proteins. The kinase phosphorylates preferentially serine or threonine residues surrounded by cluster of acidic residues. The enzyme activity is stimulated in vitro by the presence of polylysine and inhibited by heparin.
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Parasitol Today. 1993 Oct;9(10):381-4 PubMed
Biochim Biophys Acta. 1991 Nov 15;1080(3):221-6 PubMed
J Biol Chem. 1978 Feb 10;253(3):946-55 PubMed
Biochim Biophys Acta. 1988 Feb 22;968(2):211-9 PubMed
J Biol Chem. 1976 Mar 25;251(6):1799-807 PubMed
Acta Biochim Pol. 1995;42(4):405-18 PubMed
Mol Cell Biol. 1987 Oct;7(10):3409-17 PubMed
Acta Biochim Pol. 1995;42(3):357-62 PubMed
J Biol Chem. 1992 Jun 15;267(17):12061-7 PubMed
Biochim Biophys Acta. 1990 Sep 24;1054(3):267-84 PubMed
Trends Biochem Sci. 1994 Nov;19(11):439 PubMed
Biochemistry. 1997 Nov 25;36(47):14439-46 PubMed
J Biol Chem. 1981 Jul 25;256(14):7468-77 PubMed
FEBS Lett. 1996 Jan 29;379(2):153-6 PubMed
J Biol Chem. 1988 Apr 25;263(12):5499-501 PubMed
Eur J Biochem. 1990 Jan 12;187(1):89-94 PubMed
Adv Second Messenger Phosphoprotein Res. 1991;23:123-64 PubMed
J Biochem. 1985 Dec;98(6):1427-31 PubMed
J Mol Evol. 1989 Nov;29(5):448-62 PubMed
FEBS Lett. 1982 May 17;141(2):257-62 PubMed
FEBS Lett. 1987 May 11;215(2):241-6 PubMed
J Biol Chem. 1988 Jul 5;263(19):9094-101 PubMed
FEBS Lett. 1983 Aug 22;160(1-2):203-8 PubMed
Prog Nucleic Acid Res Mol Biol. 1998;59:95-133 PubMed
Eur J Biochem. 1992 May 15;206(1):259-67 PubMed
J Biol Chem. 1986 Feb 5;261(4):1868-72 PubMed
Biochem Biophys Res Commun. 1980 Jan 15;92(1):46-52 PubMed
Biochim Biophys Acta. 1988 Oct 7;971(3):332-8 PubMed
Curr Top Cell Regul. 1982;21:101-27 PubMed
Eur J Biochem. 1988 Aug 1;175(2):347-54 PubMed
Biochim Biophys Acta. 1987 Jun 15;929(1):114-6 PubMed
Biochimie. 1991 Jul-Aug;73(7-8):861-70 PubMed
FASEB J. 1995 Mar;9(5):313-23 PubMed
Mol Biol Rep. 1976 Nov;3(2):121-9 PubMed
Mol Cell Biol. 1987 Nov;7(11):4065-74 PubMed
EMBO J. 1989 Apr;8(4):1111-9 PubMed
Biochim Biophys Acta. 1996 Apr 16;1293(2):213-21 PubMed
J Biol Chem. 1987 Jan 25;262(3):1344-51 PubMed
J Biol Chem. 1984 Jun 10;259(11):7011-5 PubMed
J Biol Chem. 1982 Jun 25;257(12):6642-5 PubMed
FEBS Lett. 1981 Jun 1;128(1):33-6 PubMed
Adv Enzyme Regul. 1986;25:401-21 PubMed
Biochemistry. 1984 Jan 17;23(2):390-6 PubMed
J Biol Chem. 1986 Mar 5;261(7):3414-9 PubMed
Cell Mol Biol Res. 1994;40(5-6):411-9 PubMed
Acta Biochim Pol. 1993;40(4):497-505 PubMed
Nucleic Acids Res. 1988 Apr 25;16(8):3575 PubMed
J Biol Chem. 1979 Feb 10;254(3):762-8 PubMed
Biochem Biophys Res Commun. 1981 May 15;100(1):449-54 PubMed
Annu Rev Biochem. 1987;56:567-613 PubMed
Eur J Biochem. 1982 Oct;127(3):473-81 PubMed
Biochim Biophys Acta. 1993 Oct 3;1158(2):194-6 PubMed
J Biol Chem. 1984 Dec 10;259(23):14576-9 PubMed
J Mol Biol. 1978 Dec 5;126(2):123-40 PubMed
Biochem Biophys Res Commun. 1995 Mar 8;208(1):418-24 PubMed
Mol Cell Biol. 1990 May;10(5):2182-90 PubMed
Eur J Biochem. 1978 Mar 15;84(2):493-8 PubMed
Biochem Cell Biol. 1995 Nov-Dec;73(11-12):959-68 PubMed
Biochim Biophys Acta. 1980 Dec 15;633(3):376-85 PubMed
J Biol Chem. 1982 Sep 10;257(17):10440-5 PubMed
J Biol Chem. 1982 May 25;257(10):5359-66 PubMed
J Biol Chem. 1985 Apr 25;260(8):4745-50 PubMed
Eur J Biochem. 1981 Mar;114(3):609-13 PubMed
Eur J Biochem. 1979 Aug 1;98(2):409-16 PubMed
Acta Biochim Pol. 1996;43(2):389-96 PubMed
J Biol Chem. 1989 Feb 15;264(5):2431-7 PubMed
J Biol Chem. 1994 Jul 1;269(26):17593-9 PubMed
Eur J Biochem. 1984 Dec 17;145(3):593-9 PubMed
Arch Biochem Biophys. 1994 Mar;309(2):348-55 PubMed
Trends Biochem Sci. 1997 Jan;22(1):18-22 PubMed
Biochemistry. 1987 Dec 1;26(24):7876-83 PubMed
J Bacteriol. 1990 Feb;172(2):579-88 PubMed
Eur J Biochem. 1986 Oct 15;160(2):239-44 PubMed
Acta Biochim Pol. 1997;44(2):191-200 PubMed
J Biol Chem. 1987 Mar 15;262(8):3518-23 PubMed
Pharmacol Ther. 1993;59(1):1-30 PubMed
J Biol Chem. 1988 Aug 15;263(23):11063-6 PubMed
J Biol Chem. 1987 Jul 5;262(19):9136-40 PubMed
Eur J Biochem. 1982 May;124(1):21-35 PubMed
J Biol Chem. 1984 Mar 10;259(5):2850-5 PubMed
Eur J Biochem. 1997 Sep 1;248(2):290-5 PubMed
Annu Rev Biochem. 1991;60:717-55 PubMed
J Biol Chem. 1980 Sep 10;255(17):8038-41 PubMed
Arch Biochem Biophys. 1982 Aug;217(1):305-11 PubMed
Eur J Biochem. 1986 Aug 15;159(1):31-8 PubMed
Int Rev Cytol. 1991;124:103-36 PubMed
Biochim Biophys Acta. 1990 Aug 27;1050(1-3):51-5 PubMed
Mol Cell Biol. 1995 Sep;15(9):4754-62 PubMed
Mol Cell Endocrinol. 1983 Jun;30(3):247-66 PubMed
FEBS Lett. 1980 Nov 17;121(1):139-42 PubMed
Proc Natl Acad Sci U S A. 1976 Jun;73(6):1902-6 PubMed
Arch Biochem Biophys. 1984 Sep;233(2):540-6 PubMed
Proc Natl Acad Sci U S A. 1997 Dec 23;94(26):14500-5 PubMed
Biochim Biophys Acta. 1986 Apr 22;870(3):408-16 PubMed