Conformational and enzymatic changes of 20S proteasome of rat natural killer cells induced by mono- and divalent cations

Journal of Structural Biology

Volumn 145, Issue 3, 2004, Pages 263-271

  Reshetnyak, Yana K ^a,b   Kitson, Richard P ^a,c   Lu, Min ^a,d   Goldfarb, Ronald H ^a,c  

^a UNIVERSITY OF NORTH TEXAS HEALTH SCIENCE CENTER   (United States)

^b YALE UNIVERSITY   (United States)

^c Sopherion Therapeutics Inc   (United States)

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

Author keywords

Enzymatic activity; Mono and bivalent cations; NK cell; Proteasome; Structural analysis; Tryptophan fluorescence

Indexed keywords

CHYMOTRYPSIN; DIVALENT CATION; MONOVALENT CATION; PROTEASOME; TRYPTOPHAN;

ARTICLE; CELL LINE; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME STRUCTURE; FLUORESCENCE; LIGHT SCATTERING; NATURAL KILLER CELL; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; STRUCTURE ANALYSIS;

EID: 1042302109     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jsb.2003.11.001     Document Type: Article

References (42)

1. Baumeister W., Walz J., Zuhl F., Seemuller E. The proteasome: paradigm of a self-compartmentalizing protease. Cell. 92:1998;367-380.
2. Burstein, E.A., 1976. Adv. Sci. Technol. (Itogi Nauki i Tekhniki), ser. Biophysics, vol. 6, VINITI, Moscow, in Russian.
3. Burstein E.A., Abornev S.M., Reshetnyak Y.K. Decomposition of protein tryptophan fluorescence spectra into log-normal components: I. Algorithm of decomposition. Biophys. J. 81:2001;1699-1709.
4. Burstein E.A., Emelyanenko V.I. Log-normal description of fluorescence spectra of organic fluorophores. Photochem. Photobiol. 64:1996;316-320.
5. Bushueva T.L., Busel E.P., Burstein E.A. The interaction of protein functional groups with indole chromophore III. Amine, amide, thiol groups. Stud. Biophys. 52:1975;41-52.
6. Bushueva T.L., Busel E.P., Bushuev V.N., Burstein E.A. The interaction of protein functional groups with indole chromophore. I. Imidazole group. Stud. biophys. 44:1974;129-132.
7. Chen Yu., Barkley M.D. Toward understanding tryptophan fluorescence in proteins. Biochemistry. 37:1998;9976-9982.
8. Ciechanover A. The ubiquitin-proteasome proteolytic pathway. Cell. 79:1994;13-21.
9. Dahlmann B., Kuehn L., Grziwa A., Zwickl P., Baumeister W. Biochemical properties of the proteasome from Thermoplasma acidophilum. Eur. J. Biochem. 208:1992;789-797.
10. Dale R.E., Eisinger J. Intramolecular distances determined by energy transfer. Dependence on orientational freedom of donor acceptor. Biopolymers. 13:1974;1573-1605.
11. Djaballah H., Rivett A.J. Peptidylglutamyl-peptide hydrolase activity of the multicatalytic proteinase complex: evidence for a new high-affinity site, analysis of cooperative kinetics, and the effect of manganese ions. Biochemistry. 31:1992;4133-4141.
12. Djaballah H., Rowe A.J., Harding S.E., Rivett A.J. The multicatalytic proteinase complex (proteasome): structure and conformational changes associated with changes in proteolytic activity. Biochem. J. 292:1993;857-862.
13. Figueiredo-Pereira M.E., Chen W.E., Yuan H.M., Wilk S. A novel chymotrypsin-like component of the multicatalytic proteinase complex optimally active at acidic pH. Arch. Biochem. Biophys. 317:1995;69-78.
14. Förster A., Whitby F.G., Hill Ch.P. The pore of activated 20S proteasomes has an ordered 7-fold symmetric conformation. EMBO. 22:2003;4356-4364.
15. Goldberg A.L. Functions of the proteasome: the lysis at the end of the tunnel. Science. 268:1995;522-523.
16. Goldfarb R.H. Herberman R.B., Callewaert D.M. Mechanisms of Cytotoxicity by NK Cells. 1985;205-212 Academic Press, New York, NY.
17. Goldfarb R.H., Wasserman K., Herberman R.B., Kitson R.P. Nongranular proteolytic enzymes of rat IL-2-activated natural killer cells. I. Subcellular localization functional role. J. Immunol. 149:1992;2061-2068.
18. Groll M., Huber R. Substrate access and processing by the 20S proteasome core particle. Int. J. Biochem. Cell Biol. 35:2003;606-616.
19. Groll M., Bajorek M., Kohler A., Moroder L., Rubin D.M., Huber R., Glickman M.H., Finley D. A gated channel into the proteasome core particle. Nat. Struct. Biol. 7:2000;999-1001.
20. Groll M., Ditzel L., Lowe J., Stock D., Bochtler M., Bartunik H.D., Huber R. Structure of 20S proteasome from yeast at 2.4. Åresolution Nature. 386:1997;463-471.
21. Hudig D., Allison N.J., Ewoldt G.R., Gault R., Netski D., Pickett T.M., Redelman D., Wang M.T., Winkler U., Zunino S.J., Kam C.-M., Odake S., Power J.C. Sitkovsky M.V., Henkart P.A. Cytotoxic Cells: Recognition, Effector Function, Generation, Methods. 1993;295-304 Birkhauser, Boston, MA.
22. King R.W., Deshaies R.J., Peters J.-M., Kirschner M.W. How proteolysis drives the cell cycle. Science. 274:1996;1652-1659.
23. Kitson R.P., Lu M., Siman R., Goldfarb R.H. Proteasome inhibitor and lymphocyte function: partial inhibition of cell-mediated cytotoxicity and implication that the lymphocyte proteasome may contain multiple chymotryptic domains. In vivo. 14:2000;265-268.
24. Konev S.V. Fluorescence Phosphorescence of Proteins Nucleic Acids. 1967;Plenum Press, New York.
25. Lakowicz J.R. Principles of Fluorescence Spectroscopy. second ed. 1999;Kluwer Academic/Plenum Publishers, NewYork.
26. Lee B., Richards F.M. The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55:1971;379-400.
27. Mason R.W. Characterization of the active site of human multicatalytic proteinase. Biochem. J. 265:1990;479-484.
28. Orlowski M., Wilk S. Catalytic activities of the 20S proteasome, a multicatalytic proteinase complex. Arch. Biochem. Biophys. 383:2000;1-16.
29. Orlowski M., Cardozo Ch., Hidalgo M.C., Michaud C. Regulation of the peptidylglutamyl-peptide hydrolyzing activity of the pituitary multicatalytic proteinase complex. Biochemistry. 30:1991;5999-6005.
30. Ortiz-Navarrete V., Seelig A., Gernold M., Frentzel S., Kloetzel P.M., Hammerling G.J. Subunit of the '20S' proteasome (multicatalytic proteinase) encoded by the major histocompatibility complex. Nature. 353:1991;662-664.
31. Pereira M., Yu B., Wilk S. Enzymatic changes of the bovine pituitary multicatalytic proteinase complex, induced by magnesium ions. Arch. Biochem. Biophys. 294:1992;1-8.
32. Rechsteiner M., Realini C., Ustrell V. The proteasome activator 11 S REG (PA28) class I antigen presentation. Biochem. J. 345:2000;1-15.
33. Reshetnyak Ya.K., Burstein E.A. Decomposition of protein tryptophan fluorescence spectra into log-normal components: II. The statistical proof of discreteness of tryptophan classes in proteins. Biophys. J. 81:2001;1710-1734.
34. Reshetnyak Ya.K., Koshevnik Y., Burstein E.A. Decomposition of protein tryptophan fluorescence spectra into log-normal components: III. Correlation between fluorescence microenvironment parameters of individual tryptophan residues. Biophys. J. 81:2001;1735-1758.
35. Saitoh Y., Yokosawa H., Shin-ichi I. Sodium dodecyl sulfate-induced conformational and enzymatic changes of multicatalytic proteinase. Biochem. Biophys. Res. Commun. 162:1989;334-339.
36. Titus J.A., Perez P., Kaubisch A., Garrido M.A., Segal D.M. Human K/natural killer cells targeted with hetero-cross-linked antibodies specifically lyse tumor cells in vitro prevent tumor growth in vivo. J. Immunol. 139:1987;3153-3158.
37. Trinchieri G. Biology of natural killer cells. Adv. Immunol. 47:1989;187-376.
38. Unno M., Mizushima T., Morimoto Y., Tomisugi Y., Tanaka K., Yasouka N., Tsukihara T. The structure of the mammalian 20S proteasome at 2.75. Å resolution Structure. 10:2002;609-618.
39. Ward J.H. Hierarchical grouping to optimize an objective function. J. Am. Stat. Assoc. 58:1963.
40. Wasserman K., Kitson R.P., Rivett A.J., Sweeney S.T., Gabauer M.K., Herberman R.B., Watkins S.C., Goldfarb R.H. Nongranular proteolytic enzymes of rat IL-2-activated natural killer cells. II. Purification identification of rat A-NKP 1 A-NKP 2 as constituents of the multicatalytic proteinase (proteasome) complex. J. Cell. Biochem. 55:1994;133-145.
41. Whitby F.G., Masters E.I., Kramer L., Knowlton J.R., Yao Y., Wang C.C., Hill C.P. Structural basis for the activation of 20S proteasomes by 11S regulators. Nature. 408:2000;115-120.
42. Wilk S., Orlowski M. Evidence that pituitary cation-sensitive neutral endopeptidase is a multicatalytic protease complex. J. Neurochem. 40:1983;842-849.