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Volumn 121, Issue 4, 1997, Pages 684-689

Purification and characterization of a new ubiquitin C-terminal hydrolase (UCH-1) with isopeptidase activity from chick skeletal muscle

Author keywords

Isopeptidase; Ubiquitin C terminal hydrolase; Ubiquitin specific protease

Indexed keywords

ALDEHYDE; HYDROLASE; IODINE 125; IODOACETAMIDE; ISOENZYME; MUSCLE ENZYME; PEPTIDASE; POLYPEPTIDE; PROTEASOME; THIOL DERIVATIVE; UBIQUITIN;

EID: 0030933223     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021640     Document Type: Article
Times cited : (9)

References (33)
  • 1
    • 0029095673 scopus 로고
    • Rules of uhiquitinatiun in proteolysisamt cellular regulation
    • Wilkinsun. K.D. (1995) Rules of uhiquitinatiun in proteolysisamt cellular regulation. Annu. Km. Nutr. 15, 161-189
    • (1995) Annu. Km. Nutr. , vol.15 , pp. 161-189
    • Wilkinsun, K.D.1
  • 2
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko, A. and Cieclianover, A. (1992) The ubiquitin system for protein degradation. Annu, Rev, Biochem. 61. 761-807
    • (1992) Annu, Rev, Biochem. , vol.61 , pp. 761-807
    • Hershko, A.1    Cieclianover, A.2
  • 3
    • 0027053491 scopus 로고
    • The ubiquitin-omjugation system
    • Jentsch, S. 119921 The ubiquitin-omjugation system. Annu. Rec. Genet. 26, 179- 207
    • (1992) Annu. Rec. Genet. , vol.26 , pp. 179-207
    • Jentsch, S.1
  • 5
    • 0026089183 scopus 로고
    • Cydin is degraded by the ubiquitin pathway
    • Glotzer, M., Murray, A.W., und Kirsc'hner, M.W. (1991) Cydin is degraded by the ubiquitin pathway, Nature 349, 132-138
    • (1991) Nature , vol.349 , pp. 132-138
    • Glotzer, M.1    Murray, A.W.2    Kirsc'hner, M.W.3
  • 6
    • 0022999212 scopus 로고
    • Tho vliickrn ubiquitin gene contains a hent shock promoter and expresses an unstable mRNA in heat-shocked cells
    • Bond, U, and Schlesineier, M.J. (1986) Tho vliickrn ubiquitin gene contains a hent shock promoter and expresses an unstable mRNA in heat-shocked cells. Mal Cell. Hiol. 6. 4602-4610
    • (1986) Mal Cell. Hiol. , vol.6 , pp. 4602-4610
    • Bond, U.1    Schlesineier, M.J.2
  • 7
    • 0029162583 scopus 로고
    • Selective protein degradation: A journey's end within the proteasomc
    • JenUch, S. and Schlenkwr. S. (1995) Selective protein degradation: a journey's end within the proteasomc. Cell 82, 881-884
    • (1995) Cell , vol.82 , pp. 881-884
    • Jenuch, S.1    Schlenkwr, S.2
  • 8
    • 0028018268 scopus 로고
    • The ubiquitin-protensomi.' proteolytic pathway
    • Ciechanover, A. (1994) The ubiquitin-protensomi.' proteolytic pathway. Cell 79, 13-21
    • (1994) Cell , vol.79 , pp. 13-21
    • Ciechanover, A.1
  • 9
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomos
    • Coux, O., Tunuku, K., and uoldbcrg, A.L. (1996) Structure and functions of the 20S and 26S proteasomos. Annu. Rev. Biochem. 86,801-847
    • (1996) Annu. Rev. Biochem. , vol.86 , pp. 801-847
    • Coux, O.1    Tunuku, K.2    Uoldbcrg, A.L.3
  • 10
    • 0021679940 scopus 로고
    • The yeast ubiquitin gene: Hcnd-to-tail repeats encoding a polyubiquitin precursor protein
    • Ozkaynuk, E., Finley, D., and Vnrshavsky, A. (1984) The yeast ubiquitin gene: Hcnd-to-tail repeats encoding a polyubiquitin precursor protein. Nature 312. 663-666
    • (1984) Nature , vol.312 , pp. 663-666
    • Ozkaynuk, E.1    Finley, D.2    Vnrshavsky, A.3
  • 11
    • 0021847079 scopus 로고
    • Nucleotide sequence analysis of a cDNA encoding human ubiquitin reveals that ubiquitin is synthesized as a precursor
    • Lund, P.K., Moats-Staats, B.M., Simmons. J.G., Hoyt. E., D'Ercole, A.J., Martin, K., and van Wyk, J.J. (1985) Nucleotide sequence analysis of a cDNA encoding human ubiquitin reveals that ubiquitin is synthesized as a precursor. J. Biol. Chem. 200, 7609-7613
    • (1985) J. Biol. Chem. , vol.200 , pp. 7609-7613
    • Lund, P.K.1    Moats-Staats, B.M.2    Simmons, J.G.3    Hoyt, E.4    D'Ercole, A.J.5    Martin, K.6    Van Wyk, J.J.7
  • 12
    • 0024593537 scopus 로고
    • The tails of ubiquilin precursors are ribosomal proteins whose fusions to ubiquitin facilitate ribosome biogenesis
    • Finley, D., Uartel, B., and Varshavsky, A, (1989) The tails of ubiquilin precursors are ribosomal proteins whose fusions to ubiquitin facilitate ribosome biogenesis. Nature 338, 394-401
    • (1989) Nature , vol.338 , pp. 394-401
    • Finley, D.1    Uartel, B.2    Varshavsky, A.3
  • 14
    • 0025991456 scopus 로고
    • Cloning and functional analysis of the ubiquitin-specific protcasc UBPI of Saccharomyrex cerevisiae
    • Tobias, J.W. and Varshavsky, A. (1991) Cloning and functional analysis of the ubiquitin-specific protcasc UBPI of Saccharomyrex cerevisiae. J. Hint. Chem. 266, 12021-12028
    • (1991) J. Hint. Chem. , vol.266 , pp. 12021-12028
    • Tobias, J.W.1    Varshavsky, A.2
  • 15
    • 0026457302 scopus 로고
    • Ubiquitinspecific proteases of Saccharomyati cerevisiae: Cloning of L:HPH and UBP3, and functional analysis of the UBP guru family
    • Baker, R.T., Tobias, J.W., and Varshavsky, A. (1992) Ubiquitinspecific proteases of Saccharomyati cerevisiae: Cloning of L:HPH and UBP3, and functional analysis of the UBP guru family. J. Biol. Chem. 267, 23364-23375
    • (1992) J. Biol. Chem. , vol.267 , pp. 23364-23375
    • Baker, R.T.1    Tobias, J.W.2    Varshavsky, A.3
  • 16
    • 0027427249 scopus 로고
    • The yeast UOA-I gene encodes a deubiquitinating enzyme related to a product of the human TRE-2 oncogenc
    • Papa, F.R. and Hochstrasser, M. (1993) The yeast UOA-I gene encodes a deubiquitinating enzyme related to a product of the human TRE-2 oncogenc. Nature 366, 313-319
    • (1993) Nature , vol.366 , pp. 313-319
    • Papa, F.R.1    Hochstrasser, M.2
  • 17
    • 0024500866 scopus 로고
    • Detection, resolution, and nomenclature of multiple ubiquitin carboxyl-terminal esterases from bovine calf thymus
    • Mayor, A.N. and Wilkinson, K.D. (1989) Detection, resolution, and nomenclature of multiple ubiquitin carboxyl-terminal esterases from bovine calf thymus. Biochemistry 28, 166-172
    • (1989) Biochemistry , vol.28 , pp. 166-172
    • Mayor, A.N.1    Wilkinson, K.D.2
  • 19
    • 0026757444 scopus 로고
    • Comparisons of neuronal (PGP9.5) and non-neurmal uhiquitin C-terminal liydrolases
    • Wilkinson, K.D., Deshpandt, S., and Larsen, C.N. (1992) Comparisons of neuronal (PGP9.5) and non-neurmal uhiquitin C-terminal liydrolases. Biochim Socr. Trans. 20, 631-636
    • (1992) Biochim Socr. Trans. , vol.20 , pp. 631-636
    • Wilkinson, K.D.1    Deshpandt, S.2    Larsen, C.N.3
  • 20
    • 0028859849 scopus 로고
    • A human deubiquitinating enzyme with both isopeptidase and poptidase activities in vitro
    • Kalquet, L., Paquet, N., Fruitier. S., Hughes, G., liming-Van. K., and Jaton, .I.-C. (1990) A human deubiquitinating enzyme with both isopeptidase and poptidase activities in vitro. FEBS Lett. 359, 73-77
    • (1990) FEBS Lett. , vol.359 , pp. 73-77
    • Kalquet, L.1    Paquet, N.2    Fruitier, S.3    Hughes, G.4    Liming-Van, K.5    Jaton, I.-C.6
  • 21
    • 0028802445 scopus 로고
    • CDNA cloning of a human 100 kdDa de-ubiquitinatinig enzyme: The IGUkDa human de-ubiquitinase belongs to the ubiquitin C-terminal hydnilase family 2 (UCH2)
    • Kalquet, L., I'aqui't, N., Kruitgcr, S., Hughes. G.J., Hoang-Vnn, K., and Jaton, J.-C. (1995) cDNA cloning of a human 100 kdDa de-ubiquitinatinig enzyme: the IGUkDa human de-ubiquitinase belongs to the ubiquitin C-terminal hydnilase family 2 (UCH2). FEBS Lett. 376, 233-237
    • (1995) FEBS Lett. , vol.376 , pp. 233-237
    • Kalquet, L.1    I'aqui't, N.2    Kruitgcr, S.3    Hughes, G.J.4    Hoang-Vnn, K.5    Jaton, J.-C.6
  • 22
    • 0029561529 scopus 로고
    • Control of cell fate by a deubiquitinating enzyme encoded by the fat farcin gene
    • Huang, Y., Baker, H., and Kischer-Vize. J.A. (1995) Control of cell fate by a deubiquitinating enzyme encoded by the fat farcin gene. Science 270, 1828-1831
    • (1995) Science , vol.270 , pp. 1828-1831
    • Huang, Y.1    Baker, H.2    Kischer-Vize, J.A.3
  • 24
    • 0024378471 scopus 로고
    • Synthesis of peptiries as cloned ubiquitin extension
    • You, Y.J., Rote, K., and Rechsteiner, M. (1989) Synthesis of peptiries as cloned ubiquitin extension. J. Biol. Chem. 264, 17078-17083
    • (1989) J. Biol. Chem. , vol.264 , pp. 17078-17083
    • You, Y.J.1    Rote, K.2    Rechsteiner, M.3
  • 27
    • 0020380627 scopus 로고
    • A new solid-state reagent to iodinate proteins
    • Markwell, M.A.K. (1982) A new solid-state reagent to iodinate proteins. Anal. Biochcm. 125, 427-432
    • (1982) Anal. Biochcm. , vol.125 , pp. 427-432
    • Markwell, M.A.K.1
  • 28
    • 0000783145 scopus 로고
    • L'biquitin-aldehyde: A general inhibitor of ubiquitin-recycling processes
    • Hershko, A. and Rose, I.A. (1987) L'biquitin-aldehyde: a general inhibitor of ubiquitin-recycling processes, Proc. Natl. Acad. Sci. USA 84, 1829-1833
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1829-1833
    • Hershko, A.1    Rose, I.A.2
  • 29
    • 0342265782 scopus 로고
    • A soluble ATH-dependent proteolytic system responsible for the degradation of abnormal proteins in reticulocytus
    • Ktlinger, J.D. and Goldberg, A.L. (1977) A soluble ATH-dependent proteolytic system responsible for the degradation of abnormal proteins in reticulocytus. Proc. Natl. Acad. Sci. USA 74, 54-58
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 54-58
    • Ktlinger, J.D.1    Goldberg, A.L.2
  • 30
    • 0019841509 scopus 로고
    • Hemin inhibits ATP-dependent uhiquitin-dependent protcolysis: Role of humin in regulating ubiquitin conjugate degradation
    • Haas, A.L. and Rose, I.A. (1981) Hemin inhibits ATP-dependent uhiquitin-dependent protcolysis: role of humin in regulating ubiquitin conjugate degradation. Proc. Natl. Acad. Sci. USA 78, 6845-6848
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 6845-6848
    • Haas, A.L.1    Rose, I.A.2
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laommli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laommli, U.K.1
  • 32
    • 0023472472 scopus 로고
    • Tricine-sodium dodecylsulfate polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger, H. and Von Jagow, G. (1987) Tricine-sodium dodecylsulfate polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochern. 166, 368-379
    • (1987) Anal. Biochern. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 33
    • 0026530899 scopus 로고
    • A ubiquitin C-terminal isopeptidase that acts on polyubiquitin chains: Role in protein degradation
    • Hadari, T., Warms, J.V., Rose, I.A., and Hershko, A. (1992) A ubiquitin C-terminal isopeptidase that acts on polyubiquitin chains: Role in protein degradation. J. Biol. Chem. 267, 719-727
    • (1992) J. Biol. Chem. , vol.267 , pp. 719-727
    • Hadari, T.1    Warms, J.V.2    Rose, I.A.3    Hershko, A.4


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