Hepatitis B virus HBx peptide 116-138 and proteasome activator PA28 compete for binding to the proteasome α4/MC6 subunit

Biological Chemistry

Volumn 384, Issue 1, 2003, Pages 39-49

  Stohwasser, Ralf ^a   Holzhütter, Hermann Georg ^b   Lehmann, Undine ^a   Henklein, Peter ^b   Kloetzel, Peter M ^b  

^a German Institute   (Germany)

^b CHARITÉ UNIVERSITÄTSMEDIZIN BERLIN   (Germany)

Author keywords

20S proteasome; Activation; HBx peptide; Inhibition kinetics; Viral interference; Yeast two hybrid analysis

Indexed keywords

ENZYME ACTIVATOR; POLYPEPTIDE; PROTEASOME; PROTEIN X; VIRUS PROTEIN;

BINDING COMPETITION; BINDING SITE; CONTROLLED STUDY; ENZYME BINDING; ENZYME INACTIVATION; ENZYME SUBUNIT; HEPATITIS B VIRUS; MOUSE; NONHUMAN; PRIORITY JOURNAL; REVIEW; TWO HYBRID SYSTEM; VIRUS INTERFERENCE; YEAST;

ALGORITHMS; ANIMALS; AUTOANTIGENS; BETA-GALACTOSIDASE; BINDING, COMPETITIVE; BLOTTING, WESTERN; CLONING, MOLECULAR; DNA PRIMERS; DNA, COMPLEMENTARY; GLUTATHIONE TRANSFERASE; HEPATITIS B VIRUS; KINETICS; MICE; MULTIENZYME COMPLEXES; PEPTIDE FRAGMENTS; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN BIOSYNTHESIS; PROTEINS; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; RNA-BINDING PROTEINS; SACCHAROMYCES CEREVISIAE; TRANS-ACTIVATORS; VIRAL FUSION PROTEINS;

HEPATITIS B VIRUS;

EID: 0037226227     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2003.005     Document Type: Review

References (43)

1. Bartel, P., Chien, C. T., Sternglanz, R., and Fields, S. (1993). Elimination of false positives that arise in using the two-hybrid system. Biotechniques 14, 920-924.
2. Bochtler, M., Ditzel, L., Groll, M., Hartmann, C., and Huber, R. (1999). The proteasome. Annu. Rev. Biophys. Biomol. Struct. 28, 295-317.
3. Braun, B. C., Glickman, M., Kraft, R., Dahlmann, B., Kloetzel, P. M., Finley, D., and Schmidt, M. (1999). The base of the proteasome regulatory particle exhibits chaperone-like activity. Nature Cell Biol. 1, 221-226.
4. Coux, O., Tanaka, K., and Goldberg, A. L. (1996). Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65, 801-847.
5. DeMartino, G. N., and Slaughter, C. A. (1999). The proteasome, a novel protease regulated by multiple mechanisms. J. Biol. Chem. 274, 22123-22126.
6. Elenich, L. A., Nandi, D., Kent, A. E., McCluskey, T. S., Cruz, M., Iyer, M. N., Woodward, E. C., Conn, C. W., Ochoa, A. L., Ginsburg, D. B., and Monaco, J. J. (1999). The complete primary structure of mouse 20S proteasomes. Immunogenetics 49, 835-842.
7. Gregori, L., Fuchs, C., Figueiredo-Pereira, M. E., Van Nostrand, W. E., Goldgaber, D. (1995). Amyloid beta-protein inhibits ubiquitin-dependent protein degradation in vitro. J. Biol. Chem. 270, 19702-19708.
8. Groettrup, M., Soza, A., Eggers, M., Kuehn, L., Dick, T. P., Schild, H., Rammensee, H. G., Koszinowski, U. H., and Kloetzel, P. M. (1996). A role for the proteasome regulator PA28α in antigen presentation. Nature 381, 166-168.
9. Groll, M., Ditzel, L., Lowe, J., Stock, D., Bochtler, M., Bartunik, H. D., and Huber, R. (1997). Structure of 20S proteasome from yeast at 2.4 Å resolution. Nature 386, 463-471.
10. Groll, M., Bajorek, M., Kohler, A., Moroder, L., Rubin, D. M., Huber, R., Glickman, M. H., and Finley, D. (2000). A gated channel into the proteasome core particle. Nature Struct. Biol. 7, 1062-1067.
11. Guichet, A., Copeland, J.W.R., Erdélyi, M., Hlousek, D., Závorszky, P., Ho, J., Brown, S., Percival-Smith, A., Krause, H.M., and Ephrussi, A. (1997). The nuclear receptor homologue Ftz-F1 and the homeodomain protein Ftz are mutually dependent cofactors. Nature 385, 548-552.
12. Hendil, K. B., Khan, S., and Tanaka, K. (1998). Simultaneous binding of PA28 and PA700 activators to 20S proteasomes. Biochem. J. 332, 749-754.
13. Holzhütter, H.-G. and Colosimo, A. (1990). SIMFIT: Microcomputer software-toolkit for modellistic studies in biochemistry. Comp. Appl. Biosci. 6, 23-28.
14. Hu, Z., Zhang, Z., Doo, E., Coux, O., Goldberg, A. L., and Liang, T. J. (1999). Hepatitis B virus X protein is both a substrate and a potential inhibitor of the proteasome complex. J. Virol. 73, 7231-7240.
15. Huang, J., Kwong, J., Sun, E. C., and Liang, T. J. (1996). Proteasome complex as a potential cellular target of hepatitis B virus X protein. J. Virol. 70, 5582-5591.
16. Kania, M. A., Demartino, G. N., Baumeister, W., and Goldberg, A. L. (1996). The proteasome subunit, C2, contains an important site for binding of the PA28 (11S) activator. Eur. J. Biochem. 236, 510-516.
17. Kisselev, A. F., Akopian, T. N., Castillo, V. and Goldberg, A. L. (1999). Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown. Mol. Cell 4, 395-402.
18. Kisselev, A.F., D. Kaganovich and A.L. Goldberg (2002). Binding of hydrophobic peptides to several non-catalytic sites promotes peptide hydrolysis by all active sites of 20S proteasomes. Evidence for peptide-induced channel opening in the the α-rings. J. Biol. Chem. 277, 22260-22270.
19. Kloetzel, P. M. (2001). Antigen processing by the proteasome. Nature Rev. Mol. Cell Biol. 2, 179-187.
20. Knowlton, J. R., Johnston, S. C., Whitby, F. G., Realini, C., Zhang, Z., Rechsteiner, M., and Hill, C. P. (1997). Structure of the proteasome activator REGα (PA28α). Nature 390, 639-643.
21. Kohler, A., Bajorek, M., Groll, M., Moroder, L., Rubin, D. M., Huber, R., Glickman, M. H., and Finley, D. (2001). The substrate translocation channel of the proteasome. Biochimie 83, 325-332.
22. Luban, J., and Goff, S. P. (1995). The yeast two-hybrid system for studying protein-protein interactions. Curr. Opin. Biotechnol. 6, 59-64.
23. Miller, J. H. (1992). A Short Course in Bacterial Genetics (Cold Spring Habor, NY, USA: Cold Spring Harbor Laboratory Press).
24. Murata, S., Udono, H., Tanahashi, N., Hamada, N., Watanabe, K., Adachi, K., Yamano, T., Yui, K., Kobayashi, N., Kasahara, M., Tanaka, K. and Chiba, T. (2001). Immunoproteasome assembly and antigen presentation in mice lacking both PA28α and PA28β. EMBO J. 20, 5898-5907.
25. Ni, R., Tomita, Y., Tokunaga, F., Liang, T. J., Noda, C., Ichihara, A., and Tanaka, K. (1995). Molecular cloning of two types of cDNA encoding subunit RC6-I of rat proteasomes. Biochim. Biophys. Acta 1264, 45-52.
26. Realini, C., Dubiel, W., Pratt, G., Ferrell, K., and Rechsteiner, M. (1994). Molecular cloning and expression of a γ-interferon-inducible activator of the multicatalytic protease. J. Biol. Chem. 269, 20727-20732.
27. Realini, C., Jensen, C.C., Zhang, Z., Johnston, S.C., Knowlton, J.R., Hill, C.P. and Rechsteiner, M. (1997). Characterization of recombinant REGα, REGβ, and REGγ proteasome activators. J. Biol. Chem. 272, 25483-25492.
28. Rock, K. L., and Goldberg, A. L. (1999). Degradation of cell proteins and the generation of MHC class I-presented peptides. Annu. Rev. Immunol. 17, 739-779.
29. Schmidtke, G., Emch, S., Groettrup, M. and Holzhütter, H. G. (2000). Evidence for the existence of a non-catalytic modifier site of peptide hydrolysis by the 20S proteasome. J. Biol. Chem. 275, 22056-22063.
30. Schnall, R., G. Mannhaupt, R. Stucka, R. Tauer, S. Ehnle, C. Schwarzlose, I. Vetter and H. Feldmann, H. (1994). Identification of a set of yeast genes coding for a novel family of putative ATPases with high similarity to constituents of the 26S protease complex. Yeast 10, 1141-1155.
31. Seeger, M., Ferrell, K., Frank, R., and Dubiel, W. (1997). HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation. J. Biol. Chem. 272, 8145-8148.
32. Song, X., von Kampen, J., Slaughter, C. A., and DeMartino, G. N. (1997). Relative functions of the α and β subunits of the proteasome activator PA28. J. Biol. Chem. 272, 27994-28000.
33. Stein, R. L., Melandri, F., and Dick, L. (1996). Kinetic characterization of the chymotryptic activity of the 20S proteasome. Biochemistry 35, 3899-3908.
34. Stohwasser, R., Kuckelkorn, U., Kraft, R., Kostka, S., and Kloetzel, P. M. (1996). 20S proteasome from LMP7 knock out mice reveals altered proteolytic activities and cleavage site preferences. FEBS Lett. 383, 109-113.
35. Stohwasser, R., Salzmann, U., Giesebrecht, J., Kloetzel, P. M., and Holzhütter, H. G. (2000a). Kinetic evidences for facilitation of peptide channelling by the proteasome activator PA28. Eur. J. Biochem. 267, 6221-6230.
36. Stohwasser, R., Soza, A., Eggers, M., Koszinowski, U. H., and Kloetzel, P. (2000b). PA28αβ double and PA28β single trans-fectant mouse B8 cell lines reveal enhanced presentation of a mouse cytomegalovirus (MCMV) pp89 MHC class I epitope. Mol. Immunol. 37, 13-19.
37. Strickland, E., K. Hakala, P.J. Thomas and G.N. DeMartino. 2000. Recognition of misfolding proteins by PA700, the regulatory subcomplex of the 26 S proteasome. J. Biol. Chem. 275, 5565-5572.
38. Whitby, F. G., Masters, E. I., Kramer, L., Knowlton, J. R., Yao, Y., Wang, C. C., and Hill, C. P. (2000). Structural basis for the activation of 20S proteasomes by 11S regulators. Nature 408, 115-120.
39. Zaiss, D.M., Standera, S., Holzhuetter, H., Kloetzel, P. M. and Sijts, A.J. (1999). The proteasome inhibitor PI31 competes with PA28 for binding to 20S proteasomes. FEBS Lett. 457, 333-338.
40. Zhang, Z., Clawson, A., Realini, C., Jensen, C. C., Knowlton, J. R., Hill, C. P., and Rechsteiner, M. (1998a). Identification of an activation region in the proteasome activator REGα. Proc. Natl. Acad. Sci. USA 95, 2807-2811.
41. Zhang, Z., Realini, C., Clawson, A., Endicott,S., and Rechsteiner, M. (1998b). Proteasome activation by REG molecules lacking homolog-specific inserts. J. Biol. Chem. 273, 9501-9509.
42. Zhang, Z., Krutchinsky, A., Endicott, S., Realini, C., Rechsteiner, M., and Standing, K. G. (1999). Proteasome activator 11S REG or PA28: recombinant REG α/REG β hetero-oligomers are heptamers. Biochemistry 38, 5651-5658.
43. Zhang, Z., Torii, N., Furusaka, A., Malayaman, N., Hu, Z., and Liang, T. J. (2000). Structural and functional characterization of interaction between hepatitis B virus X protein and the proteasome complex. J. Biol. Chem. 275, 15157-65.