메뉴 건너뛰기




Volumn 291, Issue 4, 1999, Pages 997-1013

Proteasome β-type subunits: Unequal roles of propeptides in core particle maturation and a hierarchy of active site function

Author keywords

20 S proteasome; Active sites; Assembly; Propeptides; Yeast

Indexed keywords

PEPTIDE; PROTEASOME; PROTEIN SUBUNIT; UBIQUITIN;

EID: 0040008534     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2995     Document Type: Article
Times cited : (119)

References (58)
  • 1
    • 0031030057 scopus 로고    scopus 로고
    • Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum
    • Akopian T. N., Kisselev A. F., Goldberg A. L. Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum. J. Biol. Chem. 272:1997;1791-1798.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1791-1798
    • Akopian, T.N.1    Kisselev, A.F.2    Goldberg, A.L.3
  • 2
    • 0030737501 scopus 로고    scopus 로고
    • Identification of the yeast 20 S proteasome catalytic centers and subunit interactions required for active-site formation
    • Arendt C. S., Hochstrasser M. Identification of the yeast 20 S proteasome catalytic centers and subunit interactions required for active-site formation. Proc. Natl Acad. Sci. USA. 94:1997;7156-7161.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 7156-7161
    • Arendt, C.S.1    Hochstrasser, M.2
  • 3
    • 0023754392 scopus 로고
    • Cotranslational processing and protein turnover in eukaryotic cells
    • Arfin S. M., Bradshaw R. A. Cotranslational processing and protein turnover in eukaryotic cells. Biochemistry. 27:1988;7979-7984.
    • (1988) Biochemistry , vol.27 , pp. 7979-7984
    • Arfin, S.M.1    Bradshaw, R.A.2
  • 5
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair A., Finley D., Varshavsky A. In vivo half-life of a protein is a function of its amino-terminal residue. Science. 234:1986;179-186.
    • (1986) Science , vol.234 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 7
    • 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
  • 8
    • 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
  • 9
    • 0032535483 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: On protein death and cell life
    • Ciechanover A. The ubiquitin-proteasome pathway: on protein death and cell life. EMBO J. 17:1998;7151-7160.
    • (1998) EMBO J. , vol.17 , pp. 7151-7160
    • Ciechanover, A.1
  • 10
    • 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
  • 13
    • 0032569036 scopus 로고    scopus 로고
    • Conformational constraints for protein self-cleavage in the proteasome
    • Ditzel L., Huber R., Mann K., Heinemeyer W., Wolf D. H., Groll M. Conformational constraints for protein self-cleavage in the proteasome. J. Mol. Biol. 279:1998;1187-1191.
    • (1998) J. Mol. Biol. , vol.279 , pp. 1187-1191
    • Ditzel, L.1    Huber, R.2    Mann, K.3    Heinemeyer, W.4    Wolf, D.H.5    Groll, M.6
  • 14
    • 0028178515 scopus 로고
    • 20 S proteasomes are assembled via distinct precursor complexes. Processing of LMP2 and LMP7 proproteins takes place in 13-16 S preproteasome complexes
    • Frentzel S., Pesold-Hurt B., Seelig A., Kloetzel P.-M. 20 S proteasomes are assembled via distinct precursor complexes. Processing of LMP2 and LMP7 proproteins takes place in 13-16 S preproteasome complexes. J. Mol. Biol. 236:1994;975-981.
    • (1994) J. Mol. Biol. , vol.236 , pp. 975-981
    • Frentzel, S.1    Pesold-Hurt, B.2    Seelig, A.3    Kloetzel, P.-M.4
  • 15
    • 0030950435 scopus 로고    scopus 로고
    • The human alpha-type proteasomal subunit HsC8 forms a double ringlike structure, but does not assemble into proteasome-like particles with the beta-type subunits HsDelta or HsBPROS26
    • Gerards W. L. H., Enzlin J., Haner M., Hendriks I. L., Aebi U., Bloemendal H., Boelens W. The human alpha-type proteasomal subunit HsC8 forms a double ringlike structure, but does not assemble into proteasome-like particles with the beta-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.4    Aebi, U.5    Bloemendal, H.6    Boelens, W.7
  • 17
    • 0032498229 scopus 로고    scopus 로고
    • The human proteasomal subunit HsC8 induces ring formation of other alpha-type subunits
    • Gerards W. L. H., de Jong W. W., Bloemendal H., Boelens W. The human proteasomal subunit HsC8 induces ring formation of other alpha-type subunits. J. Mol. Biol. 275:1998b;113-121.
    • (1998) J. Mol. Biol. , vol.275 , pp. 113-121
    • Gerards, W.L.H.1    De Jong, W.W.2    Bloemendal, H.3    Boelens, W.4
  • 18
    • 0032483546 scopus 로고    scopus 로고
    • A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3
    • 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. 94:1998a;615-623.
    • (1998) Cell , vol.94 , pp. 615-623
    • Glickman, M.H.1    Rubin, D.M.2    Coux, O.3    Wefes, I.4    Pfeifer, G.5    Cjeka, Z.6    Baumeister, W.7    Fried, V.A.8    Finley, D.9
  • 19
    • 0031815994 scopus 로고    scopus 로고
    • The regulatory particle of the Saccharomyces cerevisiae proteasome
    • Glickman M. H., Rubin D. M., Fried V. A., Finley D. The regulatory particle of the Saccharomyces cerevisiae proteasome. Mol. Cell. Biol. 18:1998b;3149-3162.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3149-3162
    • Glickman, M.H.1    Rubin, D.M.2    Fried, V.A.3    Finley, D.4
  • 23
    • 0032584669 scopus 로고    scopus 로고
    • Mutations in the yeast proteasome β-type subunit Pre3 uncover position-dependent effects on proteasomal peptidase activity and in vivo function
    • Gueckel R., Enenkel C., Wolf D. H., Hilt W. Mutations in the yeast proteasome β-type subunit Pre3 uncover position-dependent effects on proteasomal peptidase activity and in vivo function. J. Biol. Chem. 273:1998;19443-19452.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19443-19452
    • Gueckel, R.1    Enenkel, C.2    Wolf, D.H.3    Hilt, W.4
  • 24
    • 0028152841 scopus 로고
    • C-terminal proteolytic degradation of recombinant desulfato-hirudin and its mutants in the yeast Saccharomyces cerevisiae
    • Heim J., Takabayashi K., Meyhack B., Marki W., Pohlig G. C-terminal proteolytic degradation of recombinant desulfato-hirudin and its mutants in the yeast Saccharomyces cerevisiae. Eur. J. Biochem. 226:1994;341-353.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 341-353
    • Heim, J.1    Takabayashi, K.2    Meyhack, B.3    Marki, W.4    Pohlig, G.5
  • 25
    • 0027418063 scopus 로고
    • PRE2, highly homologous to the human major histocompatibility complex-linked RING10 gene, codes for a yeast proteasome subunit necessary for chrymotryptic activity and degradation of ubiquitinated proteins
    • Heinemeyer W., Gruhler A., Möhrle V., Mahé Y., Wolf D. H. PRE2, highly homologous to the human major histocompatibility complex-linked RING10 gene, codes for a yeast proteasome subunit necessary for chrymotryptic activity and degradation of ubiquitinated proteins. J. Biol. Chem. 268:1993;5115-5120.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5115-5120
    • Heinemeyer, W.1    Gruhler, A.2    Möhrle, V.3    Mahé, Y.4    Wolf, D.H.5
  • 26
    • 0030774890 scopus 로고    scopus 로고
    • The active sites of the eukaryotic 20 S proteasome and their involvement in subunit precursor processing
    • Heinemeyer W., Fischer M., Krimmer T., Stachon U., Wolf D. H. The active sites of the eukaryotic 20 S proteasome and their involvement in subunit precursor processing. J. Biol. Chem. 272:1997;25200-26209.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25200-26209
    • Heinemeyer, W.1    Fischer, M.2    Krimmer, T.3    Stachon, U.4    Wolf, D.H.5
  • 28
    • 0029867623 scopus 로고    scopus 로고
    • Proteasomes: Destruction as a programme
    • Hilt W., Wolf D. H. Proteasomes: destruction as a programme. Trends Biochem. Sci. 21:1996;96-102.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 96-102
    • Hilt, W.1    Wolf, D.H.2
  • 29
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser M. Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 30:1996;405-439.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 31
    • 0031892541 scopus 로고    scopus 로고
    • Range of sizes of peptide products generated during degradation of different proteins by archaeal proteasomes
    • Kisselev A. F., Akopian T. N., Goldberg A. L. Range of sizes of peptide products generated during degradation of different proteins by archaeal proteasomes. J. Biol. Chem. 273:1998;1982-1989.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1982-1989
    • Kisselev, A.F.1    Akopian, T.N.2    Goldberg, A.L.3
  • 32
    • 0033525086 scopus 로고    scopus 로고
    • The sizes of peptides generated from protein by mammalian 26 and 20 S proteasomes. Implications for understanding the degradative mechanism and antigen presentation
    • Kisselev A. F., Akopian T. N., Woo K. M., Goldberg A. L. The sizes of peptides generated from protein by mammalian 26 and 20 S proteasomes. Implications for understanding the degradative mechanism and antigen presentation. J. Biol. Chem. 274:1999;3363-3371.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3363-3371
    • Kisselev, A.F.1    Akopian, T.N.2    Woo, K.M.3    Goldberg, A.L.4
  • 33
    • 0032540306 scopus 로고    scopus 로고
    • Tertiary structure formation in the propeptide of subtilisin BPN′ by successive amino acid replacements and its close relation to function
    • Kojima S., Minagawa T., Miura K. Tertiary structure formation in the propeptide of subtilisin BPN′ by successive amino acid replacements and its close relation to function. J. Mol. Biol. 277:1998;1007-1013.
    • (1998) J. Mol. Biol. , vol.277 , pp. 1007-1013
    • Kojima, S.1    Minagawa, T.2    Miura, K.3
  • 34
    • 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., 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.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 36
    • 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
  • 39
    • 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
  • 40
    • 0001730460 scopus 로고    scopus 로고
    • The 26 S proteasome
    • J.-M. Peters, J. R. Harris, & D. Finley. New York: Plenum Press
    • Rechsteiner M. The 26 S proteasome. Peters J.-M., Harris J. R., Finley D. Ubiquitin and the Biology of the Cell. 1998;Plenum Press, New York.
    • (1998) Ubiquitin and the Biology of the Cell
    • Rechsteiner, M.1
  • 41
    • 0031001763 scopus 로고    scopus 로고
    • Specific interactions between ATPase subunits of the 26 S protease
    • Richmond C., Gorbea C., Rechsteiner M. Specific interactions between ATPase subunits of the 26 S protease. J. Biol. Chem. 272:1997;13403-13411.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13403-13411
    • Richmond, C.1    Gorbea, C.2    Rechsteiner, M.3
  • 42
    • 0025979877 scopus 로고
    • Targeting, disruption, replacement, and allele rescue: Integrative DNA transformation in yeast
    • C. Guthrie, & G. R. Fink. San Diego: Academic Press Inc.
    • Rothstein R. Targeting, disruption, replacement, and allele rescue: integrative DNA transformation in yeast. Guthrie C., Fink G. R. Guide to Yeast Genetics and Molecular Biology. 1991;281-301 Academic Press Inc. San Diego.
    • (1991) Guide to Yeast Genetics and Molecular Biology , pp. 281-301
    • Rothstein, R.1
  • 43
    • 0032168508 scopus 로고    scopus 로고
    • Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome
    • Rubin D. M., Glickman M. H., Larsen C. N., Dhruvakumar S., Finley D. Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome. EMBO J. 17:1998;4909-4919.
    • (1998) EMBO J. , vol.17 , pp. 4909-4919
    • Rubin, D.M.1    Glickman, M.H.2    Larsen, C.N.3    Dhruvakumar, S.4    Finley, D.5
  • 44
    • 0030693111 scopus 로고    scopus 로고
    • Biogenesis of eukaryotic 20 S proteasomes: The complex maturation pathway of a complex enzyme
    • Schmidt M., Kloetzel P.-M. Biogenesis of eukaryotic 20 S proteasomes: the complex maturation pathway of a complex enzyme. FASEB J. 11:1997;1235-1243.
    • (1997) FASEB J. , vol.11 , pp. 1235-1243
    • Schmidt, M.1    Kloetzel, P.-M.2
  • 45
    • 0030481129 scopus 로고    scopus 로고
    • Analysis of mammalian 20 S proteasome biogenesis: The maturation of beta-subunits is an ordered two-step mechanism involving autocatalysis
    • Schmidtke G., Kraft R., Kostka S., Henklein P., Frommel C., Löwe J., Huber R., Kloetzel P.-M., Schmidt M. Analysis of mammalian 20 S proteasome biogenesis: the maturation of beta-subunits is an ordered two-step mechanism involving autocatalysis. EMBO J. 15:1996;6887-6898.
    • (1996) EMBO J. , vol.15 , pp. 6887-6898
    • Schmidtke, G.1    Kraft, R.2    Kostka, S.3    Henklein, P.4    Frommel, C.5    Löwe, J.6    Huber, R.7    Kloetzel, P.-M.8    Schmidt, M.9
  • 46
    • 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
  • 48
    • 0028881547 scopus 로고
    • The proteasome from Thermoplasma acidophilum is neither a cysteine nor a serine protease
    • Seemüller E., Lupas A., Zühl F., Zwickl P., Baumeister W. The proteasome from Thermoplasma acidophilum is neither a cysteine nor a serine protease. FEBS Letters. 359:1995b;173-178.
    • (1995) FEBS Letters , vol.359 , pp. 173-178
    • Seemüller, E.1    Lupas, A.2    Zühl, F.3    Zwickl, P.4    Baumeister, W.5
  • 49
    • 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;468-471.
    • (1996) Nature , vol.382 , pp. 468-471
    • Seemüller, E.1    Lupas, A.2    Baumeister, W.3
  • 50
    • 0025978949 scopus 로고
    • Getting started with yeast
    • C. Guthrie, & G. R. Fink. San Diego: Academic Press Inc.
    • Sherman F. Getting started with yeast. Guthrie C., Fink G. R. Guide to Yeast Genetics and Molecular Biology. 1991;3-20 Academic Press Inc. San Diego.
    • (1991) Guide to Yeast Genetics and Molecular Biology , pp. 3-20
    • Sherman, F.1
  • 51
    • 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
  • 52
    • 0026090063 scopus 로고
    • In vitro mutagenesis and plasmid shuffling: From cloned gene to mutant yeast
    • C. Guthrie, & G. R. Fink. San Diego: Academic Press Inc.
    • Sikorski R. S., Boeke J. D. In vitro mutagenesis and plasmid shuffling: from cloned gene to mutant yeast. Guthrie C., Fink G. R. Guide to Yeast Genetics and Molecular Biology. 1991;302-318 Academic Press Inc. San Diego.
    • (1991) Guide to Yeast Genetics and Molecular Biology , pp. 302-318
    • Sikorski, R.S.1    Boeke, J.D.2
  • 53
    • 0031887332 scopus 로고    scopus 로고
    • Proteasomes: Structure and biology
    • Tanaka K. Proteasomes: structure and biology. J. Biochem. (Tokyo). 123:1998;195-204.
    • (1998) J. Biochem. (Tokyo) , vol.123 , pp. 195-204
    • Tanaka, K.1
  • 54
    • 0030660073 scopus 로고    scopus 로고
    • Regulation of ubiquitin-dependent processes by deubiquitinating enzymes
    • Wilkinson K. D. Regulation of ubiquitin-dependent processes by deubiquitinating enzymes. FASEB J. 11:1997;1245-1256.
    • (1997) FASEB J. , vol.11 , pp. 1245-1256
    • Wilkinson, K.D.1
  • 55
    • 0028788228 scopus 로고
    • In vivo assembly of the proteasomal complexes, implications for antigen processing
    • Yang Y., Früh K., Ahn K., Peterson P. A. In vivo assembly of the proteasomal complexes, implications for antigen processing. J. Biol. Chem. 270:1995;27687-27694.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27687-27694
    • Yang, Y.1    Früh, K.2    Ahn, K.3    Peterson, P.A.4
  • 56
    • 0032489524 scopus 로고    scopus 로고
    • Characterization of two polyubiquitin binding sites in the 26 S protease subunit 5a
    • Young P., Deveraux Q., Beal R. E., Pickart C. M., Rechsteiner M. Characterization of two polyubiquitin binding sites in the 26 S protease subunit 5a. J. Biol. Chem. 273:1998;5461-5467.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5461-5467
    • Young, P.1    Deveraux, Q.2    Beal, R.E.3    Pickart, C.M.4    Rechsteiner, M.5
  • 57
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.