Modulation of the heat shock ubiquitin pool in Skeletonema costatum (Bacillariophyceae)

Journal of Phycology

Volumn 32, Issue 3, 1996, Pages 409-415

  Penna, Antonella ^a   Crinelli, Rita ^a   Magnani, Mauro ^a  

^a UNIVERSITY OF URBINO   (Italy)

Author keywords

Bacillariophyceae; heat stress; Skeletonema costatum; ubiquitin; ubiquitin conjugating activity

Indexed keywords

BACILLARIOPHYCEAE; SKELETONEMA COSTATUM;

EID: 0029787251     PISSN: 00223646     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.0022-3646.1996.00409.x     Document Type: Article

References (32)

1. Bond, U., Agell, N., Haas, A. L., Redman, K. & Schlesinger, M. J. 1988. Ubiquitin in stressed chicken embryo fibroblasts. J. Biol. Chem. 263:2384-8.
2. Bond, U. & Schlesinger, M. J. 1986. The chicken ubiquitin gene contains a heat shock promoter and expresses an unstable mRNA in heat-shocked cells. Mol. Cell Biol. 6:4602-10.
3. Chau, V., Tobias, J. W., Bachmair, A., Marriott, D., Ecker, D. J., Gonda, D. K. & Varshavsky, A 1989. A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science (Wash. D.C.) 243:1576-83.
4. Ciechanover, A., Heller, H., Elias, S., Haas, A. L. & Hershko, A. 1980. ATP-dependent conjugation of reticulocyte proteins with the polypeptide required for protein degradation. Proc. Nat. Acad. Sci. U.S.A. 77:1365-8.
5. Ferguson, D. L., Guikeman, J. A. & Paulsen, G. M. 1990. Ubiquitin pool modulation and protein degradation in wheat roots during high temperature stress. Plant Physiol. 92:740-6.
6. Finley, D., Bartel, B. & Varshavsky, A. 1989. The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis. Nature (Lond ) 338:394-401.
7. Finley, D., Ozkaynak, E. & Varshavsky, A. 1987. The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses. Cell 48:1035-46.
8. Ganoth, D., Leshinsky, E., Eytan, E. & Hershko, A. 1988. A multicomponent system that degrades proteins conjugated to ubiquitin. Resolution of factors and evidence for ATP-dependent complex formation. J. Biol. Chem. 263:12412-9.
9. Garbarino, J. E., Rockhold, D. R. & Belknap, W. R. 1992. Expression of stress-responsive ubiquitin genes in potato tubers. Plant Mol. Biol. 20:235-44.
10. Genschik, P., Parmentier, Y., Dun, A., Morbach, J., Criqui, M. C., Jamet, E. & Fleck, J. 1992. Ubiquitin genes are differentially regulated in protoplast-derived cultures of Nicotiana sylvestris and in response to various stresses. Plant Mol. Biol. 20:897-910.
11. Gropper, R., Brandt, R. A., Elias, S., Bearer, C. F., Mayer, A., Schwartz, A. L. & Ciechanover, A. 1991. The ubiquitin-activating enzyme, E1, is required for stress-induced lysosomal degradation of cellular proteins. J. Biol. Chem. 266: 3602-10.
12. Guillard, R. R. L. & Ryther, J. H. 1962. Studies on marine planktonic diatoms. I. Cyclotella nana Hustedt, and Detonula confervacea (Cleve) Gran. Can. J. Microbiol. 8:229-39.
13. Gurley, W. B. & Key, J. L. 1991. Transcriptional regulation of the heat-shock response: a plant perspective. Biochemistry 30: 1-12.
14. Haas, A. L. & Bright, P. M. 1985. The immunochemical detection and quantitation of intracellular ubiquitin-protein conjugates. J. Biol. Chem 260:12464-73.
15. Hershko, A. 1988. Ubiquitin-mediated protein degradation. J. Biol. Chem. 263:15237-40.
16. Hershko, A., Heller, H., Elias, S. & Ciechanover, A. 1983. Components of ubiquitin-protein ligase system: resolution, affinity purification, and role in protein breakdown. J. Biol. Chem. 258:8206-14.
17. Hough, R. F., Pratt, G. W. & Rechsteiner, M. 1988. Purification of two high molecular weight proteases from rabbit reticulocyte lysate. In Rechsteiner, M. [Ed.] Ubiquitin. Plenum Press, New York, pp. 101-34.
18. Jabben, M., Shanklin, J. & Vierstra, R. D. 1989. Ubiquitin-phytocrome conjugates: pool dynamics during in vitro phytocrome degradation. J. Biol. Chem. 264:4998-5005.
19. Johnson, E. S., Bartel, B., Seufert, W. & Varshavsky, A. 1992. Ubiquitin as a degradation signal. EMBO J. 11:497-505.
20. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.) 277:680-5.
21. Levinger, L., & Varshavsky, A. 1982. Selective arrangement of ubiquitinated and D1 protein containing nucleosomes within the Drosophila genome. Cell 28:375-85.
22. Monia, B. P., Ecker, D. J. & Crooke, S. T. 1990. New perspectives on the structure and function of ubiquitin. Biotechnology 8: 209-15.
23. Parag, H. A., Raboy, B. & Kulka, R. G. 1987. Effect of heat shock on protein degradation in mammalian cells: involvement of the ubiquitin system. EMBO J. 6:55-61.
24. Penna, A., Corsi, D., Conrad, C. & Magnani, M. 1995. Ubiquitin in Skeletonema costatum Diatom Res. 10:153-64.
25. Scoccianti, V., Penna, A., Penna, N. & Magnani, M. 1995. Effect of heat stress on polyamine content and protein pattern in Skeletonema costatum Mar. Biol. (Berl.) 121:549-54.
26. Shimogawara, K. & Muto, S. 1989. Heat shock induced change in protein ubiquitination in Chlamydomonas. Plant Cell Physiol. 30:9-16.
27. Shimogawara, K. & Muto, S. 1991. Active oxygen induced protein ubiquitination in Chlamydomonas. FEBS 278:261-2.
28. Simeon, A., van der Klei, I. J., Veenhuis, M. & Wolf, D. H. 1992. Ubiquitin, a central component of selective cytoplasmic proteolysis, is linked to proteins residing at the locus of non-selective proteolysis, the vacuole. FEBS 301:231-5.
29. Sullivan, M. L., Callis, J. & Vierstra, R. D. 1990. High performance liquid chromatography resolution of ubiquitin pathway enzymes from wheat germ. Plant. Physiol. 94:710-6.
30. Towbin, H., Stachelin, T. & Gordon, J. 1973. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Nat. Acad. Sci U.S.A. 76:4350-4.
31. Vierstra, R. D. 1987. Demonstration of ATP-dependent, ubiquitin-conjugation activities in higher plants. Plant Physiol. 84:332-6.
32. Vierstra, R. D., Langan, S. M. & Schaller, G. E. 1986. Complete amino acid sequence of ubiquitin from higher plant Avena sativa. Biochemistry 191:571-6.