Structural and functional effects of PA700 and modulator protein on proteasomes

Journal of Molecular Biology

Volumn 273, Issue 3, 1997, Pages 646-657

  Adams, George M ^a   Falke, Scott ^a   Goldberg, Alfred L ^b   Slaughter, Clive A ^c   DeMartino, George N ^d   Gogol, Edward P ^a  

^a UNIVERSITY OF MISSOURI KANSAS CITY   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

^c HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^d UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

Cooperative assembly; Electron microscopy; Enzyme regulation; Proteasome; Proteolysis control

Indexed keywords

MULTIENZYME COMPLEX; PROTEASOME; REGULATOR PROTEIN; UBIQUITIN;

ANIMAL CELL; ARTICLE; CATTLE; CONTROLLED STUDY; ELECTRON MICROSCOPY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME REGULATION; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN MODIFICATION;

ANIMALIA; BOS TAURUS;

EID: 0031592946     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1334     Document Type: Article

References (40)

1. Confalonieri F., Duguet M. A 200-amino acid ATPase module in search of a basic function. BioEssays. 17:1995;639-650.
2. Coux O., Tanaka K., Goldberg A. L. Structure and functions of the 20 S and 26 S proteasomes. Annu. Rev. Biochem. 65:1996;801-847.
3. Dahlmann B., Kopp F., Kuehn L., Niedel B., Pfeifer G., Hegerl R., Baumeister W. The multicatalytic proteinase (prosome) is ubiquitous from eukaryotes to archaebacteria. FEBS Letters. 251:1989;125-131.
4. DeMartino G. N., Slaughter C. A. Regulatory proteins of the proteasome. Enzy. Protein. 47:1993;314-324.
5. DeMartino G. N., Proske R. J., Moomaw C. R., Strong A. A., Song X., Hisamatsu H., Tanaka K., Slaughter C. A. Identification, purification, and characterization of a PA700-dependent activator of the proteasome. J. Biol. Chem. 271:1996;3112-3118.
6. Deveraux Q., Ustrell V., Pickart C., Rechsteiner M. A 26 S protease subunit that binds ubiquitin conjugates. J. Biol. Chem. 269:1994;7059-7061.
7. Dubiel W., Ferrell K., Rechsteiner M. Subunits of the regulatory complex of the 26 S protease. Mol. Biol. Reports. 21:1995;27-34.
8. Eytan E., Ganoth D., Armon T., Hershko A. ATP-dependent incorporation of 20 S protease into the 26 S complex that degrades proteins conjugated to ubiquitin. Proc. Natl Acad Sci. USA. 86:1989;7751-7755.
9. Frank J., Shimkin B., Dowse H. SPIDER: a modular software system for electron image processing. Ultramicroseopy. 6:1981a;343-358.
10. Frank J., Verschoor A., Boublik M. Computer averaging of electron micrographs of 40 S ribosomal subunits. Science. 214:1981b;1353-1355.
11. Ganoth D., Leshinsky E., Eytan E., Hershko A. A multicomponent system that degrades proteins conjugated to ubiquitin. J. Biol. Chem. 263:1988;12412-12419.
12. Groll M., Ditzel L., Löwe J., Stock D., Bochtler M., Bartunik H. D., Huber R. Structure of 20 S proteasome from yeast at 2.4 Å resolution. Nature. 386:1997;463-471.
13. Grziwa A., Baumeister W., Dahlmann B., Kopp F. Localization of subunits in proteasomes fromThermoplasma acidophilum. FEBS Letters. 290:1991;186-190.
14. Hampton R. Y., Gardner R. G., Rine J. Role of the 26 S proteasome andHRD. Mol. Biol. Cell. 7:1996;2029-2044.
15. Hilt W., Wolf D. H. Proteasomes: destruction as a programme. Trends Biochem. Sci. 21:1996;96-102.
16. Hochstrasser M. Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 30:1996;405-439.
17. Hoffman L., Pratt G., Rechsteiner M. Multiple forms of the 20 S multicatalytic and the 26 S ubiquitin-ATP-dependent proteases from rabbit reticulocyte lysate. J. Biol. Chem. 267:1992;22362-22368.
18. Hough R., Pratt G., Rechsteiner M. Purification of two high molecular weight proteases from rabbit reticulocyte lysate. J. Biol. Chem. 262:1987;8303-8313.
19. King R. W., Deshaies R. J., Peters J., Kirschner M. W. How proteolysis drives the cell cycle. Science. 274:1996;1652-1658.
20. Kominami K., Okura N., Kawamura M., DeMartino G. N., Slaughter C. A., Simbara N., Chung C. H., Fujimuro M., Yokosawa H., Shimizu Y., Tanahashi N., Tanaka K., Toh-e A. Yeast counterparts of subunits S 5a and p 58 (S3) of the human 26 S proteasome are encoded by two multicopy suppressors ofnin1-1. Mol. Biol. Cell. 8:1997;171-187.
21. Kopito R. R. ER quality control: the cytoplasmic connection. Cell. 88:1997;427-430.
22. Kopp F., Dahlmann B., Hendil K. B. Evidence indicating that the human proteasome is a complex dimer. J. Mol. Biol. 229:1993;14-19.
23. Löwe J., Stock D., Jap B., Zwickl P., Baumeister W., Huber R. Crystal structure of the 20 S proteasome from the archeonT. acidophilum. Science. 268:1995;533-539.
24. Ma C., 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 20 S proteasome. J. Biol. Chem. 269:1994;3539-3547.
25. McGuire M. J., DeMartino G. N. The latent form of macropain (high molecular weight multicatalytic protease) restores ATP-dependent proteolysis to cell-free extracts of BHK fibroblasts pretreated with antimacropain antibodies. Biochem. Biophys. Res. Commun. 160:1989;911-916.
26. Penczek P., Radermacher M., Frank J. Three-dimensional reconstruction of single particles embedded in ice. Ultramicroscopy. 40:1992;33-53.
27. Peters J., Franke W. W., Kleinschmidt J. A. Distinct 19S and 20 S subcomplexes of the 26 S proteasome and their distribution in the nucleus and the cytoplasm. J. Biol. Chem. 269:1994;7709-7718.
28. Peters J.-M., Harris J. R., Kleinschmidt J. A. Ultrastructure of the ~26 S complex containing the ~20 S cylinder particle (multicatalytic proteinase (proteasome). Eur. J. Cell Biol. 56:1991;422-432.
29. Peters J.-M., Cejka Z., Harris J. R., Kleinschmidt J. A., Baumeister W. Structural features of the 26 S proteasome complex. J. Mol. Biol. 229:1993;932-937.
30. Pühler G., Weinkauf S., Bachmann L., Müller S., Engel A., Hegerl R., Baumeister W. Subunit stoichiometry and three-dimensional arrangement in proteasomes fromThermoplasma acidophilum. EMBO J. 11:1992;1607-1616.
31. Rechsteiner M., Hoffman L., Dubiel W. The multicatalytic and 26 S proteases. J. Biol. Chem. 268:1993;6065-6068.
32. Rock K. L., Gramm C., Rothstein L., Clark K., Stein R., Dick L., Hwang D., Goldberg A. L. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell. 78:1994;761-771.
33. Tamura T., Tanaka K., Tanahashi N., Ichihara A. Improved method for preparation of ubiquitin-ligated lysozyme as substrate of ATP-dependent proteolysis. FEBS Letters. 292:1991;154-158.
34. Tanaka K., Tamura T., Yoshimura T., Ichihara A. Proteasomes: protein and gene structures. New Biolog. 4:1992;173-187.
35. Udvardy A. Purification and characterization of a multiprotein component of theDrosophila. J. Biol. Chem. 268:1993;9055-9062.
36. Ward C. L., Omura S., Kopito R. R. Degradation of CFTR by the ubiquitin-proteasome pathway. Cell. 83:1995;121-127.
37. Waxman L., Fagan J. M., Goldberg A. L. Demonstration of two distinct high molecular weight proteases in rabbit reticulocytes, one of which degrades ubiquitin conjugates. J. Biol. Chem. 262:1987;2451-2457.
38. Weber G. Protein Interactions. 1992;Chapman and Hall, New York.
39. Yoshimura T., Kameyama K., Takagi T., Ikai A., Tokunaga F., Koide T., Tanahashi N., Tamura Y., Cejka Z., Baumeister W., Tanaka K., Ichihara A. Molecular characterization of the "26 S" proteasome complex from rat liver. J. Struct. Biol. 111:1993;200-211.
40. Zwickl P., Grziwa A., Pühler G., Dahlmann B., Lottspeich F., Baumeister W. Primary structure of theThermoplasma. Biochemistry. 31:1992;964-972.