Proteins of newly isolated mutants and the amino-terminal proline are essential for ubiquitin-proteasome-catalyzed catabolite degradation of fructose-1,6-bisphosphatase of Saccharomyces cerevisiae

Journal of Biological Chemistry

Volumn 273, Issue 39, 1998, Pages 25000-25005

  Hämmerle, Marcus ^a   Bauer, Jürgen ^b,d   Rose, Matthias ^b   Szallies, Alexander ^a   Thumm, Michael ^a   Düsterhus, Stefanie ^b   Mecke, Dieter ^c   Entian, Karl Dieter ^b   Wolf, Dieter H ^a  

^a UNIVERSITY OF STUTTGART   (Germany)

^b GOETHE UNIVERSITY   (Germany)

^c UNIVERSITY OF TÜBINGEN   (Germany)

^d NESTLÉ RESEARCH CENTER   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

FRUCTOSE BISPHOSPHATASE; PROLINE; PROTEASOME; UBIQUITIN;

AMINO ACID COMPOSITION; ARTICLE; CATABOLITE REPRESSION; ENZYME DEGRADATION; ENZYME INACTIVATION; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; SACCHAROMYCES CEREVISIAE; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; BASE SEQUENCE; BIOPOLYMERS; CATALYSIS; DNA PRIMERS; ELECTROPHORESIS, GEL, PULSED-FIELD; FRUCTOSE-BISPHOSPHATASE; HYDROLYSIS; ISOCITRATE LYASE; KINETICS; MALATE DEHYDROGENASE; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PEPTIDE HYDROLASES; PHOSPHOENOLPYRUVATE CARBOXYKINASE (ATP); PHOSPHORYLATION; POLYUBIQUITIN; PROLINE; PROTEASOME ENDOPEPTIDASE COMPLEX; SACCHAROMYCES CEREVISIAE; SUBSTRATE SPECIFICITY; UBIQUITINS;

SACCHAROMYCES CEREVISIAE;

EID: 0032566737     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.273.39.25000     Document Type: Article

References (43)

1. Funayama, T., Gancedo, J. M., and Gancedo, C. (1980) Eur. J. Biochem. 109, 61-66
2. Schork, S. M., Thumm, M., and Wolf, D. H. (1995) J. Biol. Chem. 270, 26446-26450
3. Holzer, H. (1976) Trends Biochem. Sci. 1, 178-181
4. Hägele, E., Neeff, J., and Mecke, D. (1978) Eur. J. Biochem. 83, 67-76
5. Lopez-Boada, Y. S., Herrero, P., Gascon, S., and Moreno, F. (1987) Arch. Microbiol. 147, 231-234
6. Müller, M., Müller, H., and Holzer, H. (1981) J. Biol. Chem. 256, 723-727
7. Müller, D., and Holzer, H. (1981) Biochem. Biophys. Res. Commun. 103, 926-933
8. Mazon, M. J., Gancedo, J. M., and Gancedo, C. (1982) J. Biol. Chem. 257, 1128-1130
9. Pohlig, G., and Holzer, H. (1985) J. Biol. Chem. 260, 13818-13823
10. Marcus, F., Rittenhouse, J., Moberly, L., Edelstein, I., Hiller, E., and Rogers, D. T. (1988) J. Biol. Chem. 263, 6058-6062
11. Rittenhouse, J., Harrsch, P. B., Kim, J. N., and Marcus, F. (1986) J. Biol. Chem. 261, 3939-3943
12. Rittenhouse, J., Moberly, L., and Marcus, F. (1987) J. Biol. Chem. 262, 10114-10119
13. Rose, M., Entian, K. D., Hofmann, L., Vogel, R. F., and Mecke, D. (1988) FEBS Lett. 241, 55-59
14. Chiang, H. L., and Schekman, R. (1991) Nature 350, 313-318
15. Schork, S. M., Bee, G., Thumm, M., and Wolf, D. H. (1994) FEBS Lett. 349, 270-274
16. Schork, S. M., Bee, G., Thumm, M., and Wolf, D. H. (1994) Nature 369, 283-284
17. Entian, K. D., Droll, L., and Mecke, D. (1983) Arch. Microbiol. 134, 187-192
18. Gamo, F. J., Navas, M. A., Blazquez, M. A., Gancedo, C., and Gancedo, J. M. (1994) Eur. J. Biochem. 222, 879-884
19. Ordiz, I., Herrero, P., Rodicio, R., and Moreno, F. (1995) FEBS Lett. 367, 219-222
20. Bachmair, A., Finley, D., and Varshavsky, A. (1986) Science 234, 179-186
21. Richter-Ruoff, B., Heinemeyer, W., and Wolf, D. H. (1992) FEBS Lett. 302, 192-196
22. Myers, A. M., Tzagoloff, A., Kinney, D. M., and Lusty, C. J. (1986) Gene (Amst.) 45, 299-310
23. Zweimüller, M. (1990) Dissertation, Johann Wolfgang Goethe-Universität Frankfurt
24. Hochstrasser, M., Ellison, M. J., Chau, V., and Varshavsky, A. (1991) Proc. Natl. Sci. U. S. A. 88, 4606-4610
25. Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
26. Christianson, T. W., Sikorski, R. S., Dante, M., Shero, J. H., and Hieter, P. (1992) Gene (Amst.) 110, 119-122
27. Kunkel, T. A., Roberts, J. D., and Zakour, R. A. (1987) Methods Enzymol. 154, 367-382
28. Fink, G. R. (1970) Methods Enzymol. 17, 59-78
29. Ciriacy, M. (1975) Mol. Gen. Genet. 138, 157-163
30. Gancedo, J. M., and Gancedo, C. (1971) Arch. Microbiol. 76, 132-138
31. Dixon, G. H., and Kornberg, H. L. (1959) Biochem. J. 72, 3-7
32. Wolfe, R. G., and Neilands, J. B. (1956) J. Biol. Chem. 221, 61-69
33. Hansen, R. J., Hinze, H., and Holzer, H. (1976) Anal. Biochem. 74, 576-584
34. Chaudhuri, B., Hämmerle, M., and Fürst, P. (1995) FEBS Lett. 357, 221-226
35. Zamenhoff, S. (1957) Methods Enzymol. 3, 696-704
36. Guarente, L. (1983) Methods Enzymol. 101, 181-191
37. Heinemeyer, W., Kleinschmidt, J. A., Saidowsky, J., Escher, C., and Wolf, D. H. (1991) EMBO J. 10, 555-562
38. Fischer, M., Hilt, W., Richter-Ruoff, B., Gonen, H., Ciechanover, A., and Wolf, D. H. (1994) FEBS Lett. 355, 69-75
39. Haarasilta, S., and Oura, E. (1975) Eur. J. Biochem. 52, 1-7
40. Witt, I., Kronau, R., and Holzer, H. (1966) Biochim. Biophys. Acta 128, 63-73
41. Duntze, W., Neumann, D., and Holzer, H. (1968) Eur. J. Biochem. 3, 326-331
42. Heinemeyer, W., Fischer, M., Krimmer, T., Stachon, U., and Wolf, D. H. (1997) J. Biol. Chem. 272, 25200-25209
43. Johnson, E. S., Bartel, B., Seufert, W., and Varshavsky, A. (1992) EMBO J. 11, 497-505