Brassica napus hsp90 can autophosphorylate and phosphorylate other protein substrates

Molecular and Cellular Biochemistry

Volumn 185, Issue 1-2, 1998, Pages 33-38

  Park, Mahnhoon ^a   Yong Kang, C ^a   Krishna, Priti ^a  

^a UNIVERSITY OF WESTERN ONTARIO   (Canada)

Author keywords

Brassica napus; hsp90; Phosphorylation; Protein kinase

Indexed keywords

ADENOSINE TRIPHOSPHATE; ANTISERUM; CASEIN; COMPLEMENTARY DNA; HEAT SHOCK PROTEIN 90; HISTONE; MANGANESE; PHOSPHORUS 32; PHOSPHOSERINE; RECOMBINANT PROTEIN; VEGETABLE PROTEIN;

ANIMAL CELL; ARTICLE; AUTOPHOSPHORYLATION; BRASSICA; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; IMMUNOBLOTTING; INSECT; NONHUMAN; PLANT; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION;

ANIMALS; BRASSICA; CASEINS; CATTLE; HISTIDINE; HISTONES; HSP90 HEAT-SHOCK PROTEINS; PHOSPHOAMINO ACIDS; PHOSPHORYLATION; PLANT PROTEINS; RECOMBINANT PROTEINS; SERINE; SERUM ALBUMIN, BOVINE; SUBSTRATE SPECIFICITY;

ANIMALIA; BRASSICA; BRASSICA NAPUS; INSECTA;

EID: 7344241532     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1006884306169     Document Type: Article

References (28)

1. Hendrick JP, Hartl F-U: Molecular chaperone functions of heat-shock proteins. Ann Rev Biochem 62: 349-384, 1993
2. Parsell DA, Lindquist S: The functions of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins. Ann Rev Genet 27: 437-496, 1993
3. Pratt WB: The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor. J Biol Chem 268: 21455-21458, 1993
4. Picard D, Khursheed B, Garabedian MJ, Fortin MG, Lindquist S, Yamamoto KR: Reduced levels of hsp90 compromise steroid receptor action in vivo. Nature 348: 166-168, 1990
5. src with the cellular proteins pp50 and pp90. Curr Top Microbiol Immunol 123: 1-22, 1986
6. Miyata Y, Yahara I: The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity. J Biol Chem 267: 7042-7047, 1992
7. Csermely P, Kahn CR: The 90-kDa heat shock protein (hsp90) possesses an ATP binding site and autophosphorylating activity. J Biol Chem 266: 4943-4950, 1991
8. Nadeau K, Das A, Walsh CT: Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases. J Biol Chem 268: 1479-1487, 1993
9. Csermely P, Kajtar J, Hollosi M, Jalsovszky G, Holly S, Kahn CR, Gergely P, Soti C, Mihaly K, Somogyi J: ATP induces a conformational change of the 90-kDa heat shock protein (hsp90). J Biol Chem 268: 1901-1907, 1993
10. Dechert U, Weber P, Konig B, Ortwein C, Nilson I, Linxweiler W, Wollny E, Gassen HG: A protein kinase isolated from porcine brain microvessels is similar to a class of heat-shock proteins. Eur J Biochem 225: 805-809, 1994
11. Szyszka R, Kramer G, Hardesty B: The phosphorylation state of the reticulocyte 90-kDa heat shock protein affects its ability to increase phosphorylation of peptide initiation factor 2 a subunit by the hemesensitive kinase. Biochemistry 28: 1435-1438, 1989
12. Conner TW, Lafayette PR, Nagao RT, Key JL: Sequence and expression of a HSP83 from Arabidopsis thaliana. Plant Physiol 94: 1689-1695, 1990
13. Koning AJ, Rose R, Comai L: Developmental expression of tomato heat-shock cognate protein 80. Plant Physiol 100: 801-811, 1992
14. Felsheim RF, Das A: Structure and expression of a heat-shock protein 83 gene of Pharbitis nil. Plant Physiol 100: 1764-1771, 1992
15. Marrs KAE, Casey ES, Capitant SA, Bouchard RA, Dietrich PS, Mettler U, Sinibaldi RM: Characterization of two maize hsp90 heat shock protein genes and expression during heat shock, embryogenesis, and pollen development. Dev Genet 14: 27-41, 1993
16. Krishna P, Sacco M, Cherutti JF, Hill S: Cold-induced accumulation of hsp90 transcripts in Brassica napus. Plant Physiol 107: 915-923, 1995
17. LiY, Luo L,Thomas D, Kang CY: Control of expression, glycosylation, and secretion of HIV-1 gp120 by homologous and heterologous signal sequences. Virology 204: 266-278, 1994
18. Kitts PA, Possee RD: A method for producing recombinant baculovirus expression vectors at high frequency. Biotechniques 14: 810-816, 1993
19. Laemmli UK: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685, 1970
20. Krishna P, Reddy RK, Sacco M, Frappier JRH, Felsheim RF: Analysis of the native forms of the 90 kDa heat shock protein (hsp90) in plant cytosolic extracts. Plant Mol Biol 33: 457-466, 1997
21. Csermely P, Kajtar J, Hollosi M, Oikarinen J, Somogyi J: The 90 kDa heat shock protein (hsp90) induces the condensation of the chromatin structure. Biochem Biophys Res Commun 202: 1657-1663, 1994
22. Rose DW, Welch WJ, Kramer G, Hardesty B: Possible involvement of the 90-kDa heat shock protein in the regulation of protein synthesis. J Biol Chem 264: 6239-6244, 1989
23. Stancato LF, Chow Y-H, Hutchison KA Perdew GH, Jove R, Pratt WB: Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system. J Biol Chem 268: 21711-21716, 1993
24. Aligue R, Akhavan-Niak H, Russell P: A role for hsp90 in cell cycle control: Weel tyrosine kinase activity requires interaction with hsp90. EMBO J 13: 6099-6106, 1994
25. Cutforth T, Rubin GM: Mutations in hsp83 and cdc37 impair signaling by the sevenless receptor tyrosine kinase in Drosophila. Cell 77: 1027-1036, 1994
26. Stancato LF, Hutchison KA, Krishna P, Pratt WB: Animal and plant cell lysates share a conserved chaperone system that assembles the glucocorticoid receptor into a functional heterocomplex with hsp90. Biochemistry 35: 554-561, 1996
27. Dittmar KD, Demady DR, Stancato LF, Krishna P, Pratt WB: Folding of the glucocorticoid receptor by the hsp90-based chaperone machinery: The role of p23 is to dynamically stabilize receptor hsp90 heterocomplexes formed by hsp90-p60-hsp70. J Biol Chem 272: 21213-21220, 1997
28. Owens-Grillo JK, Stancato LF, Hoffmann K, Pratt WB, Krishna P: Binding of immunophilins to the 90 kDa heat shock protein (hsp90) via a tetratricopeptiderepeat domain is a conserved protein interaction in plants. Biochemistry 35: 15249-15255, 1996