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Volumn 335, Issue 1, 2004, Pages 233-245

Crystal structures of the Rhodococcus proteasome with and without its pro-peptides: Implications for the role of the pro-peptide in proteasome assembly

Author keywords

Assembly activation; Inter subunit contacts; Pro peptide; Proteasome assembly; Rhodococcus erythropolis

Indexed keywords

BACTERIAL PROTEIN; MUTANT PROTEIN; PROTEASOME; PROTEIN PRECURSOR;

EID: 0344687318     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.08.029     Document Type: Article
Times cited : (70)

References (40)
  • 2
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20 S and 26 S proteasomes
    • 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.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 3
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome, a molecular machine designed for controlled proteolysis
    • Voges D., Zwickl P., Baumeister W. The 26S proteasome, a molecular machine designed for controlled proteolysis. Annu. Rev. Biochem. 68:1999;1015-1068.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 4
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • Baumeister W., Walz J., Zühl F., Seemüller E. The proteasome: paradigm of a self-compartmentalizing protease. Cell. 92:1998;367-380.
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zühl, F.3    Seemüller, E.4
  • 6
    • 0029328494 scopus 로고
    • The first characterization of eubacterial proteasome: The 20 S complex of Rhodococcus
    • Tamura T., Nagy I., Lupas A., Lottspeich F., Cejka Z., Schoofs G., et al. The first characterization of eubacterial proteasome: the 20 S complex of Rhodococcus. Curr. Biol. 5:1995;766-774.
    • (1995) Curr. Biol. , vol.5 , pp. 766-774
    • Tamura, T.1    Nagy, I.2    Lupas, A.3    Lottspeich, F.4    Cejka, Z.5    Schoofs, G.6
  • 7
    • 0033083967 scopus 로고    scopus 로고
    • Proteasomes and other self-compartmentalizing proteases in prokaryotes
    • De Mot R., Nagy I., Walz J., Baumeister W. Proteasomes and other self-compartmentalizing proteases in prokaryotes. Trends Microbiol. 7:1999;88-92.
    • (1999) Trends Microbiol. , vol.7 , pp. 88-92
    • De Mot, R.1    Nagy, I.2    Walz, J.3    Baumeister, W.4
  • 8
    • 0036092394 scopus 로고    scopus 로고
    • Molecular evolution of proteasomes
    • pp. 1-22. P. Zwickl, & W. Baumeister. Berlin, Heidelberg: Springer-Verlag
    • pp. 1-22 Volker C., Lupas A. Molecular evolution of proteasomes. Zwickl P., Baumeister W. The Proteasome-Ubiquitin Protein Degradation Pathway. 2002;Springer-Verlag, Berlin, Heidelberg.
    • (2002) The Proteasome-Ubiquitin Protein Degradation Pathway
    • Volker, C.1    Lupas, A.2
  • 9
    • 0029042511 scopus 로고
    • Crystal structure of the 20 S proteasome from the archaeon T. acidophilum at 3.4 Å resolution
    • Löwe J., Stock D., Jap B.K., Zwickl P., Baumeister W., Huber R. Crystal structure of the 20 S proteasome from the archaeon T. acidophilum at 3. 4 Å resolution. Science. 268:1995;533-539.
    • (1995) Science , vol.268 , pp. 533-539
    • Löwe, J.1    Stock, D.2    Jap, B.K.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 12
    • 0033613196 scopus 로고    scopus 로고
    • The catalytic sites of 20 S proteasomes and their role in subunit maturation: A mutational and crystallographic study
    • Groll M., Heinemeyer W., Jäger S., Ullrich T., Bochtler M., Wolf D.H., Huber R. The catalytic sites of 20 S proteasomes and their role in subunit maturation: a mutational and crystallographic study. Proc. Natl Acad. Sci. USA. 96:1999;10976-10983.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 10976-10983
    • Groll, M.1    Heinemeyer, W.2    Jäger, S.3    Ullrich, T.4    Bochtler, M.5    Wolf, D.H.6    Huber, R.7
  • 13
  • 14
    • 0024308135 scopus 로고
    • Proteolytic processing and physiological regulation
    • Neurath H. Proteolytic processing and physiological regulation. Trends Biochem. Sci. 14:1989;268-271.
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 268-271
    • Neurath, H.1
  • 15
    • 0027421103 scopus 로고
    • Intramolecular chaperones and protein folding
    • Shinde U., Inouye M. Intramolecular chaperones and protein folding. Trends Biochem. Sci. 18:1993;442-446.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 442-446
    • Shinde, U.1    Inouye, M.2
  • 16
    • 0029019483 scopus 로고
    • Pro-sequence-assisted protein folding
    • Eder J., Fersht A.R. Pro-sequence-assisted protein folding. Mol. Microbiol. 16:1995;609-614.
    • (1995) Mol. Microbiol. , vol.16 , pp. 609-614
    • Eder, J.1    Fersht, A.R.2
  • 18
    • 0032054714 scopus 로고    scopus 로고
    • The role of assembly in insulin's biosynthesis
    • Dodson G., Steiner D. The role of assembly in insulin's biosynthesis. Curr. Opin. Struct. Biol. 8:1998;189-194.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 189-194
    • Dodson, G.1    Steiner, D.2
  • 19
    • 4243580491 scopus 로고    scopus 로고
    • Self-processing of subunits of the proteasome
    • Seemüller E., Zwickl P., Baumeister W. Self-processing of subunits of the proteasome. The Enzymes. 22:2001;335-371.
    • (2001) The Enzymes , vol.22 , pp. 335-371
    • Seemüller, E.1    Zwickl, P.2    Baumeister, W.3
  • 20
    • 0029789918 scopus 로고    scopus 로고
    • Autocatalytic processing of the 20 S proteasome
    • Seemüller E., Lupas A., Baumeister W. Autocatalytic processing of the 20 S proteasome. Nature. 382:1996;468-470.
    • (1996) Nature , vol.382 , pp. 468-470
    • Seemüller, E.1    Lupas, A.2    Baumeister, W.3
  • 21
    • 0039660001 scopus 로고    scopus 로고
    • Dissecting the assembly pathway of the 20 S proteasome
    • Zühl F., Seemüller E., Golbik R., Baumeister W. Dissecting the assembly pathway of the 20 S proteasome. FEBS Letters. 418:1997;189-194.
    • (1997) FEBS Letters , vol.418 , pp. 189-194
    • Zühl, F.1    Seemüller, E.2    Golbik, R.3    Baumeister, W.4
  • 22
    • 0030595329 scopus 로고    scopus 로고
    • Autocatalytic subunit processing couples active site formation in the 20 S proteasome to completion of assembly
    • Chen P., Hochstrasser M. Autocatalytic subunit processing couples active site formation in the 20 S proteasome to completion of assembly. Cell. 86:1996;961-972.
    • (1996) Cell , vol.86 , pp. 961-972
    • Chen, P.1    Hochstrasser, M.2
  • 23
    • 0028907938 scopus 로고
    • Genes encoded in the major histocompatibility complex affecting the generation of peptides for TAP transport
    • Cerundolo V., Kelly A., Elliot T., Trowsdale A. Genes encoded in the major histocompatibility complex affecting the generation of peptides for TAP transport. Eur. J. Immunol. 25:1995;554-562.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 554-562
    • Cerundolo, V.1    Kelly, A.2    Elliot, T.3    Trowsdale, A.4
  • 26
    • 0030950435 scopus 로고    scopus 로고
    • The human α-type proteasomal subunit HsC8 forms a double ring-like structure, but does not assemble into proteasome-like particles with the β-type subunits HsDelta or HsBPROS26
    • Gerards W.L.H., Enzlin J., Haner M., Hendriks I.L.A.M., Aebi U., Bloemendal H., Boelens W. The human α-type proteasomal subunit HsC8 forms a double ring-like structure, but does not assemble into proteasome-like particles with the β-type subunits HsDelta or HsBPROS26. J. Biol. Chem. 272:1997;10080-10086.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10080-10086
    • Gerards, W.L.H.1    Enzlin, J.2    Haner, M.3    Hendriks, I.L.A.M.4    Aebi, U.5    Bloemendal, H.6    Boelens, W.7
  • 27
    • 0033408417 scopus 로고    scopus 로고
    • α5 Subunit in Trypanosoma brucei proteasome can self-assemble to form a cylinder of four stacked heptamer rings
    • Yao Y., Toth C.R., Huang L., Wong M.L., Dias P., Burlingame A.L., et al. α5 Subunit in Trypanosoma brucei proteasome can self-assemble to form a cylinder of four stacked heptamer rings. Biochem. J. 344:1999;349-358.
    • (1999) Biochem. J. , vol.344 , pp. 349-358
    • Yao, Y.1    Toth, C.R.2    Huang, L.3    Wong, M.L.4    Dias, P.5    Burlingame, A.L.6
  • 28
    • 0030880547 scopus 로고    scopus 로고
    • Intermediates in the formation of mouse 20 S proteasomes: Implications for the assembly of precursor β subunits
    • Nandi D., Woodward E., Ginsburg D.B., Monaco J.J. Intermediates in the formation of mouse 20 S proteasomes: implications for the assembly of precursor β subunits. EMBO J. 16:1997;5363-5375.
    • (1997) EMBO J. , vol.16 , pp. 5363-5375
    • Nandi, D.1    Woodward, E.2    Ginsburg, D.B.3    Monaco, J.J.4
  • 29
    • 0031585998 scopus 로고    scopus 로고
    • Maturation of mammalian 20 S proteasome: Purification and characterization of 13 S and 16 S proteasome precursor complexes
    • Schmidtke G., Schmidt M., Kloetzel P.-M. Maturation of mammalian 20 S proteasome: purification and characterization of 13 S and 16 S proteasome precursor complexes. J. Mol. Biol. 268:1997;95-106.
    • (1997) J. Mol. Biol. , vol.268 , pp. 95-106
    • Schmidtke, G.1    Schmidt, M.2    Kloetzel, P.-M.3
  • 30
    • 0032548998 scopus 로고    scopus 로고
    • Ump1p is required for proper maturation of the 20 S proteasome and becomes its substrate upon completion of the assembly
    • Ramos P.C., Höckendorff J., Johnson E.S., Varshavsky A., Dohmen R.J. Ump1p is required for proper maturation of the 20 S proteasome and becomes its substrate upon completion of the assembly. Cell. 92:1998;489-499.
    • (1998) Cell , vol.92 , pp. 489-499
    • Ramos, P.C.1    Höckendorff, J.2    Johnson, E.S.3    Varshavsky, A.4    Dohmen, R.J.5
  • 33
    • 0037436376 scopus 로고    scopus 로고
    • Investigations on the maturation and regulation of archaebacterial proteasomes
    • Groll M., Brandstetter H., Bartunik H., Bourenkow G., Huber R. Investigations on the maturation and regulation of archaebacterial proteasomes. J. Mol. Biol. 327:2003;75-83.
    • (2003) J. Mol. Biol. , vol.327 , pp. 75-83
    • Groll, M.1    Brandstetter, H.2    Bartunik, H.3    Bourenkow, G.4    Huber, R.5
  • 37
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.-Y., Cowan S.W., Kjeldgaad M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaad, M.4
  • 38
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of proteins structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of proteins structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 39
    • 0028057108 scopus 로고
    • Raster3D version 2.0. A program for photorealistic molecular graphics
    • Merritt E.A., Murphy M.E. Raster3D version 2.0. A program for photorealistic molecular graphics. Acta Crystallog. sect. D. 50:1994;869-873.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.2
  • 40
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins. 11:1991;281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3


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