Rapid isolation and characterization of the yeast proteasome regulatory complex

Biochemical and Biophysical Research Communications

Volumn 273, Issue 2, 2000, Pages 509-515

  Saeki, Yasushi ^a   Toh E, Akio ^b   Yokosawa, Hideyoshi ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

Author keywords

19S regulatory complex; 26S proteasome; Base complex; Immunoaffinity chromatography; Lid complex; Multiubiquitin chain binding; Yeast

Indexed keywords

FUNGAL PROTEIN; PROTEASOME;

ARTICLE; ENZYME BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN ISOLATION; YEAST;

EID: 0343081478     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.2000.2980     Document Type: Article

References (23)

1. Hershko A., Ciechanover A. The ubiquitin system. Annu. Rev. Biochem. 67:1998;425-479.
2. Coux O., Tanaka K., Goldberg A. L. Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65:1996;801-847.
3. Baumeister W., Waltz J., Zuhl F., Seemuller E. The proteasome: Paradigm of a self-compartmentalizing protease. Cell. 92:1998;367-380.
4. DeMartino G. N., Slaughter C. A. The proteasome, a novel protease regulated by multiple mechanisms. J. Biol. Chem. 274:1999;22123-22126.
5. Voges D., Zwickl P., Baumeister W. The 26S proteasome: A molecular machine designed for controlled proteolysis. Annu. Rev. Biochem. 68:1999;1015-1068.
6. Groll M., Ditzel L., Lowe J., Stock D., Bochtler M., Bartunik H. D., Huber R. Structure of 20S proteasome from yeast at 2.4 A resolution. Nature. 386:1997;463-471.
7. Glickman M. H., Rubin D. M., Fried V. A., Finley D. The regulatory particle of the Saccharomyces cerevisiae proteasome. Mol. Cell. Biol. 18:1998;3149-3162.
8. Glickman M. H., Rubin D. M., Coux O., Wefes I., Pfeifer G., Cjeka Z., Baumeister W., Fried V. A., Finley D. A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3. Cell. 94:1998;615-623.
9. Ferrell K., Wilkinson C. R. M., Dubiel W., Gordon C. Regulatory subunit interactions of the 26S proteasome, a complex problem. Trends Biochem. Sci. 25:2000;83-88.
10. van Nocker S., Sadis S., Rubin D. M., Glickman M., Fu H., Coux O., Wefes I., Finley D., Vierstra R. D. The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover. Mol. Cell. Biol. 16:1996;6020-6028.
11. Kominami K., Okura N., Kawamura M., DeMartino G. N., Slaughter C. A., Shimbara N., Chung C. H., Fujimuro M., Yokosawa H., Shimizu Y., Tanahashi N., Tanaka K., Toh-e A. Yeast counterparts of subunits S5a and p58 (S3) of the human 26S proteasome are encoded by two multicopy suppressors of nin1-1. Mol. Biol. Cell. 8:1997;171-187.
12. Fu H., Sadies S., Rubin D. M., Glickmann M., van Nocker S., Finley D., Vierstra R. D. Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26 S proteasome subunit Mcb1. J. Biol. Chem. 273:1998;1970-1981.
13. Sutton A., Immanuel D., Arndt K. T. The SIT4 protein phosphatase functions in late G1 for progression into S phase. Mol. Cell. Biol. 11:1991;2133-2148.
14. Sherman F. Getting started with yeast. Methods Enzymol. 194:1991;3-21.
15. Tanaka K., Yoshimura T., Kumatori A., Ichihara A., Ikai A., Nishigai M., Kameyama K., Takagi T. Proteasomes (multi-protease complexes) as 20S ring-shaped particles in a variety of eukaryotic cells. J. Biol. Chem. 263:1988;16209-16217.
16. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
17. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
18. Takeuchi J., Fujimuro M., Yokosawa H., Tanaka K., Toh-e A. Rpn9 is required for efficient assembly of the yeast 26S proteasome. Mol. Cell. Biol. 19:1999;6575-6584.
19. Fujimuro M., Takada H., Saeki Y., Toh-e A., Tanaka K., Yokosawa H. Growth-dependent change of the 26S proteasome in budding yeast. Biochem. Biophys. Res. Commun. 251:1998;818-823.
20. Kominami K., DeMartino G. N., Moomaw C. R., Slaughter C. A., Shimbara N., Fujimuro M., Yokosawa H., Hisamatsu H., Tanahashi N., Shimizu Y., Tanaka K., Toh-e A. Nin1p, a regulatory subunit of the 26S proteasome, is necessary for activation of Cdc28p kinase of Saccharomyces cerevisiae. EMBO J. 14:1995;3105-3115.
21. Chu-Ping M., Vu J. H., Proske R. J., Slaughter C. A., DeMartino G. N. Identification, purification, and characterization of a high molecular weight, ATP-dependent activator (PA700) of the 20S proteasome. J. Biol. Chem. 269:1994;3539-3547.
22. DeMartino G. N., Moomaw C. R., Zagnitko O. P., Proske R. J., Chu-Ping M., Afendis S. J., Swaffield J. C., Slaughter C. A. PA700, an ATP-dependent activator of the 20 S proteasome, is an ATPase containing multiple members of a nucleotide-binding protein family. J. Biol. Chem. 269:1994;20878-20884.
23. Braun B. C., Glickman M., Kraft R., Dahlmann B., Kloetzel P.-M., Finley D., Schmidt M. The base of the proteasome regulatory particle exhibits chaperone-like activity. Nature Cell Biol. 1:1999;221-226.