The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related Hsp70 family

Journal of Biological Chemistry

Volumn 279, Issue 21, 2004, Pages 21992-22001

  Shaner, Lance ^a   Trott, Amy ^a   Goeckeler, Jennifer L ^b   Brodsky, Jeffrey L ^b   Morano, Kevin A ^a  

^a UNIVERSITY OF TEXAS MEDICAL SCHOOL   (United States)

^b UNIVERSITY OF PITTSBURGH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; POLYPEPTIDES; YEAST;

PEPTIDE BINDING DOMAINS (PBD); PEPTIDE SUBSTRATES;

BIOCHEMISTRY;

ADENOSINE TRIPHOSPHATASE; AMINO ACID; ASPARAGINE; ASPARTIC ACID; CHAPERONE; GLUTAMINE; GLYCINE; HEAT SHOCK PROTEIN 110; HEAT SHOCK PROTEIN 70; LYSINE; NUCLEOTIDE; PROTEIN SSE1; UNCLASSIFIED DRUG;

ALLELE; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; CONTROLLED STUDY; FUNGUS GROWTH; GENETIC COMPLEMENTATION; HYDROLYSIS; IMMUNOPRECIPITATION; MOLECULAR INTERACTION; MUTATION; PHENOTYPE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STABILITY; STRUCTURE ACTIVITY RELATION; YEAST;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; ALLELES; BETA-GALACTOSIDASE; BLOTTING, WESTERN; CYCLOHEXIMIDE; GENETIC COMPLEMENTATION TEST; HSP110 HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; HYDROLYSIS; IMMUNOBLOTTING; KINETICS; MODELS, BIOLOGICAL; MUTATION; PEPTIDES; PHENOTYPE; PLASMIDS; PRECIPITIN TESTS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; PROTEIN SYNTHESIS INHIBITORS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SEPHAROSE; STRUCTURE-ACTIVITY RELATIONSHIP; TEMPERATURE; TIME FACTORS; TRANSCRIPTION, GENETIC;

FUNGI; MAMMALIA;

EID: 2542435778     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M313739200     Document Type: Article

References (38)

1. Craig, E. A., Baxter, B. K., Becker, J., Halladay, J., and Ziegelhoffer, T. (1994) in The Biology of Heat Shock Proteins and Molecular Chaperones (Morimoto, R. I., Tissieres, A., and Georgopolos, C., eds) Vol. 26, pp. 31-52, Cold Spring Harbor Laboratory Press, New York
2. Craven, R. A., Egerton, M., and Stirling, C. J. (1996) EMBO J. 15, 2640-2650
3. Liberek, K., Skowyra, D., Zylicz, M., Johnson, C., and Georgopoulos, C. (1991) J. Biol. Chem. 266, 14491-14496
4. Zhu, X., Zhao, X., Burkholder, W. F., Gragerov, A., Ogata, C. M., Gottesman, M. E., and Hendrickson, W. A. (1996) Science 272, 1606-1614
5. Schroder, H., Langer, T., Hartl, F. U., and Bukau, B. (1993) EMBO J. 12, 4137-4144
6. Bolliger, L., Deloche, O., Glick, B. S., Georgopoulos, C., Jeno, P., Kronidou, N., Horst, M., Morishima, N., and Schatz, G. (1994) EMBO J. 13, 1998-2006
7. Easton, D. P., Kaneko, Y., and Subjeck, J. R. (2000) Cell Stress Chaperones 5, 276-290
8. Craven, R. A., Tyson, J. R., and Stirling, C. J. (1997) Trends Cell Biol. 7, 277-282
9. Oh, H. J., Chen, X., and Subjeck, J. R. (1997) J. Biol. Chem. 272, 31636-31640
10. Oh, H. J., Easton, D., Murawski, M., Kaneko, Y., and Subjeck, J. R. (1999) J. Biol. Chem. 274, 15712-15718
11. Ishihara, K., Yamagishi, N., Saito, Y., Adachi, H., Kobayashi, Y., Sobue, G., Ohtsuka, K., and Hatayama, T. (2003) J. Biol. Chem. 278, 25143-25150
12. Mukai, H., Kuno, T., Tanaka, H., Hirata, D., Miyakawa, T., and Tanaka, C. (1993) Gene (Amst.) 132, 57-66
13. Shirayama, M., Kawakami, K., Matsui, Y., Tanaka, K., and Toh-e, A. (1993) Mol. Gen. Genet. 240, 323-332
14. Brodsky, J. L., Werner, E. D., Dubas, M. E., Goeckeler, J. L., Kruse, K. B., and McCracken, A. A. (1999) J. Biol. Chem. 274, 3453-3460
15. Goeckeler, J. L., Stephens, A., Lee, P., Caplan, A. J., and Brodsky, J. L. (2002) Mol. Biol. Cell 13, 2760-2770
16. Liu, X. D., Morano, K. A., and Thiele, D. J. (1999) J. Biol. Chem. 274, 26654-26660
17. Wei, J., Gaut, J. R., and Hendershot, L. M. (1995) J. Biol. Chem. 270, 26677-26682
18. McClellan, A. J., and Brodsky, J. L. (2000) Genetics 156, 501-512
19. McClellan, A. J., Endres, J. B., Vogel, J. P., Palazzi, D., Rose, M. D., and Brodsky, J. L. (1998) Mol. Biol. Cell 9, 3533-3545
20. Flaherty, K. M., Wilbanks, S. M., DeLuca-Flaherty, C., and McKay, D. B. (1994) J. Biol. Chem. 269, 12899-12907
21. Wilbanks, S. M., DeLuca-Flaherty, C., and McKay, D. B. (1994) J. Biol. Chem. 269, 12893-12898
22. Lee-Yoon, D., Easton, D., Murawski, M., Burd, R., and Subjeck, J. R. (1995) J. Biol. Chem. 270, 15725-15733
23. Kaiser, C., Michaelis, S., and Mitchell, A. (eds) (1994) Methods in Yeast Genetics, Cold Spring Harbor Laboratory Press, New York
24. Mumberg, D., Muller, R., and Funk, M. (1995) Gene (Amst.) 156, 119-122
25. Aiyar, A., Xiang, Y., and Leis, J. (1996) Methods Mol. Biol. 57, 177-191
26. Duina, A. A., Kalton, H. M., and Gaber, R. F. (1998) J. Biol. Chem. 273, 18974-18978
27. Santoro, N., Johansson, N., and Thiele, D. J. (1998) Mol. Cell. Biol. 18, 6340-6352
28. Lu, Z., and Cyr, D. M. (1998) J. Biol. Chem. 273, 27824-27830
29. Freeman, B. C., Myers, M. P., Schumacher, R., and Morimoto, R. I. (1995) EMBO J. 14, 2281-2292
30. Scheufler, C., Brinker, A., Bourenkov, G., Pegoraro, S., Moroder, L., Bartunik, H., Hartl, F. U., and Moarefi, I. (2000) Cell 101, 199-210
31. Sousa, M. C., and McKay, D. B. (1998) Biochemistry 37, 15392-15399
32. Davis, J. E., Voisine, C., and Craig, E. A. (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 9269-9276
33. Han, W., and Christen, P. (2003) Biochem. J. 369, 627-634
34. Moro, F., Fernandez, V., and Muga, A. (2003) FEBS Lett. 533, 119-123
35. Montgomery, D. L., Morimoto, R. I., and Gierasch, L. M. (1999) J. Mol. Biol. 286, 915-932
36. Wang, X. Y., Chen, X., Oh, H. J., Repasky, E., Kazim, L., and Subjeck, J. (2000) FEBS Lett. 465, 98-102
37. Chou, C. C., Forouhar, F., Yeh, Y. H., Shr, H. L., Wang, C., and Hsiao, C. D. (2003) J. Biol. Chem. 278, 30311-30316
38. Wei, J., and Hendershot, L. M. (1995) J. Biol. Chem. 270, 26670-26676