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Volumn 267, Issue 12, 2000, Pages 3712-3722

Molecular characterization of the thermosensitive E1 ubiquitin- activating enzyme cell mutant A31N-ts20. Requirements upon different levels of e1 for the ubiquitination/degradation of the various protein substrates in vivo

Author keywords

Somatic mammalian cells; Ubiquitin activating enzyme; Ubiquitin protein conjugates; Ubiquitin E1

Indexed keywords

UBIQUITIN PROTEIN LIGASE;

EID: 0033937208     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01404.x     Document Type: Article
Times cited : (45)

References (33)
  • 2
    • 0030016595 scopus 로고    scopus 로고
    • Structure and function of the 20S and 26S proteasomes
    • 2. Coux, O., Tanaka, K. & Goldberg, A.L. (1996) Structure and function of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65, 801-847.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 3
    • 0029162583 scopus 로고
    • Selective protein degradation: A journey's end within the proteasome
    • 3. Jentsch, S. & Schlenker, S. (1995) Selective protein degradation: a journey's end within the proteasome. Cell 82, 881-884.
    • (1995) Cell , vol.82 , pp. 881-884
    • Jentsch, S.1    Schlenker, S.2
  • 4
    • 0002370251 scopus 로고    scopus 로고
    • The ubiquitin-conjugation system
    • (Peters, J.-M., Harris, J.R. & Finley, D., eds), Plenum Press, New York, USA
    • 4. Scheffner, M., Smith, S. & Jentsch, S. (1998) The ubiquitin-conjugation system. In Ubiquitin and the Biology of the Cell (Peters, J.-M., Harris, J.R. & Finley, D., eds), pp. 65-91. Plenum Press, New York, USA.
    • (1998) Ubiquitin and the Biology of the Cell , pp. 65-91
    • Scheffner, M.1    Smith, S.2    Jentsch, S.3
  • 5
    • 0025831142 scopus 로고
    • A candidate spermatogenesis gene on the mouse Y chromosome is homologous to ubiquitin-activating enzyme E1
    • 5. Kay, G.F., Ashworth, A., Penny, A., Dunlop. G.D., Swift, M., Brockdorff, N. & Rastan, S. (1992) A candidate spermatogenesis gene on the mouse Y chromosome is homologous to ubiquitin-activating enzyme E1. Nature 354, 486-489.
    • (1992) Nature , vol.354 , pp. 486-489
    • Kay, G.F.1    Ashworth, A.2    Penny, A.3    Dunlop, G.D.4    Swift, M.5    Brockdorff, N.6    Rastan, S.7
  • 6
    • 0025790212 scopus 로고
    • Homology of a candidate spermatogenic gene from the mouse Y chromosome to the ubiquitin-activating enzyme E1
    • 6. Mitchell, M.J., Woods, D.R., Tucker, P.K., Opp. J.S. & Bishop, C.E. (1992) Homology of a candidate spermatogenic gene from the mouse Y chromosome to the ubiquitin-activating enzyme E1. Nature 354, 483-486.
    • (1992) Nature , vol.354 , pp. 483-486
    • Mitchell, M.J.1    Woods, D.R.2    Tucker, P.K.3    Opp, J.S.4    Bishop, C.E.5
  • 7
    • 0026769411 scopus 로고
    • Multiple forms of ubiquitin-activating enzyme E1 from wheat
    • 7. Hatfield, P.M. & Vierstra, R.D. (1992) Multiple forms of ubiquitin-activating enzyme E1 from wheat. J. Biol. Chem. 267, 14799-14803.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14799-14803
    • Hatfield, P.M.1    Vierstra, R.D.2
  • 8
    • 0031080458 scopus 로고    scopus 로고
    • The ubiquitin-activating enzyme (E1) gene family in Arabidopsis thaliana
    • 8. Hatfield, P.M., Gosink, M.M., Carpenter, T.B. & Vierstra, R.D. (1997) The ubiquitin-activating enzyme (E1) gene family in Arabidopsis thaliana. Plant J. 11, 216-226.
    • (1997) Plant J. , vol.11 , pp. 216-226
    • Hatfield, P.M.1    Gosink, M.M.2    Carpenter, T.B.3    Vierstra, R.D.4
  • 9
    • 0025967290 scopus 로고
    • UBA1: An essential yeast gene encoding ubiquitin-activating enzyme
    • 9. McGrath, J.P., Jentsch, S. & Varshavsky, A. (1991) UBA1: an essential yeast gene encoding ubiquitin-activating enzyme. EMBO J. 10, 227-236.
    • (1991) EMBO J. , vol.10 , pp. 227-236
    • McGrath, J.P.1    Jentsch, S.2    Varshavsky, A.3
  • 10
    • 0028205667 scopus 로고
    • Accumulation of p53 in a mutant cell line defective in the ubiquitin pathway
    • 10. Chowdary, D.R., Bermody, J.J., Jha, K.K. & Ozer, H.L. (1994) Accumulation of p53 in a mutant cell line defective in the ubiquitin pathway. Mol. Cell Biol. 14, 1997-2003.
    • (1994) Mol. Cell Biol. , vol.14 , pp. 1997-2003
    • Chowdary, D.R.1    Bermody, J.J.2    Jha, K.K.3    Ozer, H.L.4
  • 11
    • 0023775756 scopus 로고
    • A Chinese hamster cell cycle mutant arrested at G2 phase has a temperature-sensitive ubiquitin-activating enzyme E1
    • 11. Kulka, R.G., Raboy, B., Schuster, R., Parag, H.A., Diamond, A., Ciechanover, A. & Marcus, M. (1988) A Chinese hamster cell cycle mutant arrested at G2 phase has a temperature-sensitive ubiquitin-activating enzyme E1. J. Biol. Chem. 263, 15726-15731.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15726-15731
    • Kulka, R.G.1    Raboy, B.2    Schuster, R.3    Parag, H.A.4    Diamond, A.5    Ciechanover, A.6    Marcus, M.7
  • 12
    • 0025253775 scopus 로고
    • Ubiquitin metabolism in ts85 cells, a mouse carcinoma cell line that contains a thermolabile ubiquitin activating enzyme
    • 12. Deveraux, Q., Wells, R. & Rechsteiner, M. (1990) Ubiquitin metabolism in ts85 cells, a mouse carcinoma cell line that contains a thermolabile ubiquitin activating enzyme. J. Biol. Chem. 265, 6323-6329.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6323-6329
    • Deveraux, Q.1    Wells, R.2    Rechsteiner, M.3
  • 13
    • 0003694904 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, USA
    • 13. Harlow, E. & Lane, D. (1988) Antibodies. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, USA.
    • (1988) Antibodies
    • Harlow, E.1    Lane, D.2
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 14. Laemmli, U.K. (1971) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1971) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0029068172 scopus 로고
    • Ubiquitinylation is not an absolute requirement for degradation of c-jun protein by the 26S proteasome
    • 15. Jariel-encontre, I., Pariat, M., Martin, F., Carillo, S., Salvat, C. & Piechaczyk, M. (1995) Ubiquitinylation is not an absolute requirement for degradation of c-jun protein by the 26S proteasome. J. Biol. Chem. 270, 11623-11627.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11623-11627
    • Jariel-Encontre, I.1    Pariat, M.2    Martin, F.3    Carillo, S.4    Salvat, C.5    Piechaczyk, M.6
  • 16
    • 0026664253 scopus 로고
    • Immunodetection, microscopic localization of the ubiquitin-activating enzyme E1 in HepG2 cells
    • 16. Schwarz, A.L., Traush, J.S., Ciechanover, A. & Geuze, J.W. (1992) Immunodetection, microscopic localization of the ubiquitin-activating enzyme E1 in HepG2 cells. Proc. Natl Acad. Sci. USA 89, 5542-5546.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 5542-5546
    • Schwarz, A.L.1    Traush, J.S.2    Ciechanover, A.3    Geuze, J.W.4
  • 17
    • 0027411355 scopus 로고
    • Isolation of human p53 specific monoclonal antibodies and their use in immunohistochemical studies of tumor cells
    • 17. Legros, Y., Lacabanne, V., d'Agay, M.F., Larsen, C.J., Pla, M. & Soussi, T. (1993) Isolation of human p53 specific monoclonal antibodies and their use in immunohistochemical studies of tumor cells. Bull. Fr. Cancer 80, 102-110.
    • (1993) Bull. Fr. Cancer , vol.80 , pp. 102-110
    • Legros, Y.1    Lacabanne, V.2    D'Agay, M.F.3    Larsen, C.J.4    Pla, M.5    Soussi, T.6
  • 18
    • 0021099710 scopus 로고
    • Components of the ubiquitin-protein ligase system. Resolution, affinity purification and role in protein breakdown
    • 18. Hershko, A., Heller, H., Elias, S. & Ciechanover, A. (1983) Components of the ubiquitin-protein ligase system. Resolution, affinity purification and role in protein breakdown. J. Biol. Chem. 258, 8206-8214.
    • (1983) J. Biol. Chem. , vol.258 , pp. 8206-8214
    • Hershko, A.1    Heller, H.2    Elias, S.3    Ciechanover, A.4
  • 19
    • 0022718902 scopus 로고
    • Conjugation of ubiquitin to cellular proteins in permeabilized mammalian cells: Comparison of mitotic and interphase cells
    • 19. Raboy, B., Parag, H.A. & Kulka, R.G. (1986) Conjugation of ubiquitin to cellular proteins in permeabilized mammalian cells: comparison of mitotic and interphase cells. EMBO J. 5, 863-869.
    • (1986) EMBO J. , vol.5 , pp. 863-869
    • Raboy, B.1    Parag, H.A.2    Kulka, R.G.3
  • 20
    • 0032524621 scopus 로고    scopus 로고
    • Characterization of human hect domain family members and their interaction with UbcH5 and UbcH7
    • 20. Schwarz, S.E., Rosa, J.L. & Scheffner, M. (1998) Characterization of human hect domain family members and their interaction with UbcH5 and UbcH7. J. Biol. Chem. 273, 12148-12154.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12148-12154
    • Schwarz, S.E.1    Rosa, J.L.2    Scheffner, M.3
  • 21
    • 0021177121 scopus 로고
    • Characterization of a ts mutant of BALB/3T3 cells and correction of the defect by in vitro addition of extracts from wild-type cells
    • 21. Zeng, G.C., Donegan, J., Ozer, H.L. & Hand, R. (1984) Characterization of a ts mutant of BALB/3T3 cells and correction of the defect by in vitro addition of extracts from wild-type cells. Mol. Cell. Biol. 4, 1815-1822.
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 1815-1822
    • Zeng, G.C.1    Donegan, J.2    Ozer, H.L.3    Hand, R.4
  • 22
    • 0008608694 scopus 로고
    • (Rao, R.N., Johnson, R.T. & Sperling, K., eds), Academic Press, Orlando, FL, USA
    • 22. Marcus, M. & Hirschberg, J. (1982) Premature Chromosome Condensation. (Rao, R.N., Johnson, R.T. & Sperling, K., eds), pp. 173-194. Academic Press, Orlando, FL, USA.
    • (1982) Premature Chromosome Condensation , pp. 173-194
    • Marcus, M.1    Hirschberg, J.2
  • 23
    • 0029952441 scopus 로고    scopus 로고
    • In vivo ubiquitination and proteasome-mediated degradation of p53
    • 23. Maki, C.G., Huibregtse, J. & Howley, P. (1996) In vivo ubiquitination and proteasome-mediated degradation of p53. Cancer Res. 56, 2649-2654.
    • (1996) Cancer Res. , vol.56 , pp. 2649-2654
    • Maki, C.G.1    Huibregtse, J.2    Howley, P.3
  • 24
    • 0022338010 scopus 로고
    • Core histone variants and ubiquitinated histones 2A and 2B of rat cerebral cortex neurons
    • 24. Pina, B. & Suau, P. (1985) Core histone variants and ubiquitinated histones 2A and 2B of rat cerebral cortex neurons. Biochem. Biophys. Res. Commun. 133, 505-510.
    • (1985) Biochem. Biophys. Res. Commun. , vol.133 , pp. 505-510
    • Pina, B.1    Suau, P.2
  • 25
    • 0027228196 scopus 로고
    • Characterization of DNA synthesis at a restrictive temperature in the temperature-sensitive mutant, tsFT5 cells, that belong to the complementation group of ts85 cells containing a thermolabile ubiquitin-activating enzyme E1. Involvment of the ubiquitin-conjugating system in DNA replication
    • 25. Mori, M., Eki, T., Takahashi-Kudo, M., Hanaoka, F., Ui, M. & Enomoto, T. (1993) Characterization of DNA synthesis at a restrictive temperature in the temperature-sensitive mutant, tsFT5 cells, that belong to the complementation group of ts85 cells containing a thermolabile ubiquitin-activating enzyme E1. Involvment of the ubiquitin-conjugating system in DNA replication. J. Biol. Chem. 268, 16803-16809.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16803-16809
    • Mori, M.1    Eki, T.2    Takahashi-Kudo, M.3    Hanaoka, F.4    Ui, M.5    Enomoto, T.6
  • 26
    • 0028027308 scopus 로고
    • Ubiquitin-dependent c-jun degradation in vivo is mediated by the δ domain
    • 26. Treier, M., Staszewsk, L.M. & Bohman, D. (1994) Ubiquitin-dependent c-jun degradation in vivo is mediated by the δ domain. Cell 78, 787-798.
    • (1994) Cell , vol.78 , pp. 787-798
    • Treier, M.1    Staszewsk, L.M.2    Bohman, D.3
  • 27
    • 0032560789 scopus 로고    scopus 로고
    • Differential directing of c-Fos and c-Jun proteins to the proteasome in serum-stimulated mouse embryo fibroblasts
    • 27. Salvat, C., Jariel-Encontre, I., Acquaviva, C., Omura, S. & Piechaczyk, M. (1998) Differential directing of c-Fos and c-Jun proteins to the proteasome in serum-stimulated mouse embryo fibroblasts. Oncogene 17, 327-337.
    • (1998) Oncogene , vol.17 , pp. 327-337
    • Salvat, C.1    Jariel-Encontre, I.2    Acquaviva, C.3    Omura, S.4    Piechaczyk, M.5
  • 28
    • 0019305278 scopus 로고
    • A temperature-sensitive mutant of cultured mouse cells defective for chromosome condensation
    • 28. Mita, S., Yasuda, H., Marunouchi, Y., Ishiko, S. & Yamasa, M. (1980) A temperature-sensitive mutant of cultured mouse cells defective for chromosome condensation. Exp. Cell Res. 126, 407-116.
    • (1980) Exp. Cell Res. , vol.126 , pp. 407-1116
    • Mita, S.1    Yasuda, H.2    Marunouchi, Y.3    Ishiko, S.4    Yamasa, M.5
  • 29
    • 0028834782 scopus 로고
    • Degradation of the proto-oncogene product c-fos by the ubiquitin proteolytic system in vivo and in vitro; identification and characterization of the conjugating enzymes
    • 29. Stancovski, I., Gonen, H., Orian, A., Schwartz, A.L. & Ciechanover, A. (1995) Degradation of the proto-oncogene product c-fos by the ubiquitin proteolytic system in vivo and in vitro; identification and characterization of the conjugating enzymes. Mol. Cell Biol. 15, 7106-7116.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 7106-7116
    • Stancovski, I.1    Gonen, H.2    Orian, A.3    Schwartz, A.L.4    Ciechanover, A.5
  • 30
    • 0023802469 scopus 로고
    • The resolution and characterization of putative ubiquitin carrier protein isozymes from rabbit reticulocytes
    • 30. Haas, A.L. & Bright, P.M. (1988) The resolution and characterization of putative ubiquitin carrier protein isozymes from rabbit reticulocytes. J. Biol. Chem. 263, 13258-13267.
    • (1988) J. Biol. Chem. , vol.263 , pp. 13258-13267
    • Haas, A.L.1    Bright, P.M.2
  • 31
    • 0021812747 scopus 로고
    • Identification of ubiquitinated histone 2A and 2B in Physarum polycephalum. Disappearance of these proteins at metaphase and reappearance at anaphase
    • 31. Mueller, R.D., Yasuda, H., Hatch, C.L., Bonner, W.M. & Bradbury, E. (1985) Identification of ubiquitinated histone 2A and 2B in Physarum polycephalum. Disappearance of these proteins at metaphase and reappearance at anaphase. J. Biol. Chem. 260, 5147-5153.
    • (1985) J. Biol. Chem. , vol.260 , pp. 5147-5153
    • Mueller, R.D.1    Yasuda, H.2    Hatch, C.L.3    Bonner, W.M.4    Bradbury, E.5
  • 32
    • 0008585058 scopus 로고
    • Disappearance of a structural chromatin A24 in mitosis: Implication for molecular basis of chromatin condensation
    • 32. Martsui, S.I., Seon, B.K. & Sandberg, A. (1974) Disappearance of a structural chromatin A24 in mitosis: implication for molecular basis of chromatin condensation. Proc. Natl Acad. Sei. USA 76, 6386-6390.
    • (1974) Proc. Natl Acad. Sei. USA , vol.76 , pp. 6386-6390
    • Martsui, S.I.1    Seon, B.K.2    Sandberg, A.3


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