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Volumn 16, Issue 8, 1996, Pages 4064-4072

A novel rat homolog of the Saccharomyces cerevisiae ubiquitin- conjugating enzymes UBC4 and UBC5 with distinct biochemical features is induced during spermatogenesis

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; COMPLEMENTARY DNA; MESSENGER RNA; UBIQUITIN CONJUGATING ENZYME;

EID: 0029898412     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.16.8.4064     Document Type: Article
Times cited : (52)

References (33)
  • 2
    • 0028233372 scopus 로고
    • Purification and characterization of a novel species of ubiquitin-carrier protein, E2, that is involved in degradation of non-N-end rule protein substrates
    • Blumenfeld, N., H. Gonen, A. Mayer, C. E. Smith, N. R. Siegel, A. L. Schwartz, and A. Ciechanover. 1994. Purification and characterization of a novel species of ubiquitin-carrier protein, E2, that is involved in degradation of non-N-end rule protein substrates. J. Biol. Chem. 269:9574-9581.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9574-9581
    • Blumenfeld, N.1    Gonen, H.2    Mayer, A.3    Smith, C.E.4    Siegel, N.R.5    Schwartz, A.L.6    Ciechanover, A.7
  • 3
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P., and N. Sacchi. 1987. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:155-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 155-159
    • Chomczynski, P.1    Sacchi, N.2
  • 4
    • 0028018268 scopus 로고
    • The ubiquitin-proteasome proteolytic pathway
    • Ciechanover, A. 1994. The ubiquitin-proteasome proteolytic pathway. Cell 79:13-21.
    • (1994) Cell , vol.79 , pp. 13-21
    • Ciechanover, A.1
  • 5
    • 0001996305 scopus 로고
    • Cell biology of mammalian spermiogenesis
    • C. Desjardins (ed.), Oxford University Press, New York
    • Clermont, Y., R. Oko, and L. Hermo. 1993. Cell biology of mammalian spermiogenesis, p. 332-375. In C. Desjardins (ed.), Cell and molecular biology of the testis. Oxford University Press, New York.
    • (1993) Cell and Molecular Biology of the Testis , pp. 332-375
    • Clermont, Y.1    Oko, R.2    Hermo, L.3
  • 6
    • 0027788114 scopus 로고
    • Tertiary structures of class I ubiquitin-conjugating enzymes are highly conserved: Crystal structure of yeast Ubc4
    • Cook, W. J., L. C. Jeffrey, Y. Xu, and V. Chau. 1993. Tertiary structures of class I ubiquitin-conjugating enzymes are highly conserved: crystal structure of yeast Ubc4. Biochemistry 32:13809-13817.
    • (1993) Biochemistry , vol.32 , pp. 13809-13817
    • Cook, W.J.1    Jeffrey, L.C.2    Xu, Y.3    Chau, V.4
  • 7
    • 0027582362 scopus 로고
    • Homologs of the essential ubiquitin conjugating enzymes UBC1, 4, and 5 in yeast are encoded by a multigene family in Arabidopsis thaliana
    • Girod, P. A., T. B. Carpenter, S. van Nocker, M. L. Sullivan, and R. D. Vierstra. 1993. Homologs of the essential ubiquitin conjugating enzymes UBC1, 4, and 5 in yeast are encoded by a multigene family in Arabidopsis thaliana. Plant J. 3:545-552.
    • (1993) Plant J. , vol.3 , pp. 545-552
    • Girod, P.A.1    Carpenter, T.B.2    Van Nocker, S.3    Sullivan, M.L.4    Vierstra, R.D.5
  • 8
    • 0023802469 scopus 로고
    • The resolution and characterization of putative ubiquitin carrier protein isozymes from rabbit reticulocytes
    • Haas, A. L., and P. M. Bright. 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
  • 9
    • 0020478717 scopus 로고
    • Ubiquitin-activating enzyme: Mechanism and role in protein-ubiquitin conjugation
    • Haas, A. L., J. V. B. Warms, A. Hershko, and I. A. Rose. 1982. Ubiquitin-activating enzyme: mechanism and role in protein-ubiquitin conjugation. J. Biol. Chem. 257:2543-2548.
    • (1982) J. Biol. Chem. , vol.257 , pp. 2543-2548
    • Haas, A.L.1    Warms, J.V.B.2    Hershko, A.3    Rose, I.A.4
  • 12
    • 0029588670 scopus 로고
    • Identification of a family of closely related human ubiquitin conjugating enzymes
    • Jensen, J. P., P. W. Bates, M. Yang, R. D. Vierstra, and A. M. Weissman. 1995. Identification of a family of closely related human ubiquitin conjugating enzymes. J. Biol. Chem. 270:30408-30414.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30408-30414
    • Jensen, J.P.1    Bates, P.W.2    Yang, M.3    Vierstra, R.D.4    Weissman, A.M.5
  • 13
    • 0027053491 scopus 로고
    • The ubiquitin-conjugation system
    • Jentsch, S. 1992. The ubiquitin-conjugation system. Annu. Rev. Genet. 26: 179-207.
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 179-207
    • Jentsch, S.1
  • 14
    • 0025831142 scopus 로고
    • A candidate spermatogenesis gene on the mouse Y chromosome is homologous to ubiquitin-activating enzyme E1
    • Kay, G. F., A. Ashworth, G. D. Penny, M. Dunlop, S. Swift, N. Brockdorff, and S. Rastan. 1991. A candidate spermatogenesis gene on the mouse Y chromosome is homologous to ubiquitin-activating enzyme E1. Nature (London) 354:486-489.
    • (1991) Nature (London) , vol.354 , pp. 486-489
    • Kay, G.F.1    Ashworth, A.2    Penny, G.D.3    Dunlop, M.4    Swift, S.5    Brockdorff, N.6    Rastan, S.7
  • 15
    • 0000768803 scopus 로고
    • Improvements in the coating technique of radioautography
    • Kopriwa, B. M. L., and C. P. Leblond. 1962. Improvements in the coating technique of radioautography. J. Histochem. Cytochem. 10:269-284.
    • (1962) J. Histochem. Cytochem. , vol.10 , pp. 269-284
    • Kopriwa, B.M.L.1    Leblond, C.P.2
  • 16
    • 0017366616 scopus 로고
    • Separation of spermatogenic cells and nuclei from rodent testes
    • D. Prescott (ed.), Academic Press, New York
    • Meistrich, M. L. 1977. Separation of spermatogenic cells and nuclei from rodent testes, p. 15-54. In D. Prescott (ed.), Methods in cell biology. Academic Press, New York.
    • (1977) Methods in Cell Biology , pp. 15-54
    • Meistrich, M.L.1
  • 17
    • 0025790212 scopus 로고
    • Homology of a candidate spermatogenic gene from the mouse Y chromosome to the ubiquitin-activating enzyme E1
    • Mitchell, M. J., D. R. Woods, P. K. Tucker, J. S. Opp, and C. E. Bishop. 1991. Homology of a candidate spermatogenic gene from the mouse Y chromosome to the ubiquitin-activating enzyme E1. Nature (London) 354:483-489.
    • (1991) Nature (London) , vol.354 , pp. 483-489
    • Mitchell, M.J.1    Woods, D.R.2    Tucker, P.K.3    Opp, J.S.4    Bishop, C.E.5
  • 18
    • 0021809123 scopus 로고
    • Nature and function of endocytosis in Sertoli cells of the rat
    • Morales, C., Y. Clermont, and L. Hermo. 1985. Nature and function of endocytosis in Sertoli cells of the rat. Am. J. Anat. 173:203-217.
    • (1985) Am. J. Anat. , vol.173 , pp. 203-217
    • Morales, C.1    Clermont, Y.2    Hermo, L.3
  • 19
    • 0025866561 scopus 로고
    • Cytoplasmic localization during storage and translation of the mRNAs of transition protein 1 and protamine 1, two translationally regulated transcript of the mammalian testis
    • Morales, C. R., Y. K. Kwon, and N. B. Hecht. 1991. Cytoplasmic localization during storage and translation of the mRNAs of transition protein 1 and protamine 1, two translationally regulated transcript of the mammalian testis. J. Cell Sci. 100:119-131.
    • (1991) J. Cell Sci. , vol.100 , pp. 119-131
    • Morales, C.R.1    Kwon, Y.K.2    Hecht, N.B.3
  • 20
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P. H. 1975. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250:4007-4021.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 21
    • 0021996450 scopus 로고
    • Functional heterogeneity of ubiquitin carrier proteins
    • Pickart, C. M., and I. A. Rose. 1985. Functional heterogeneity of ubiquitin carrier proteins. J. Biol. Chem. 260:1573-1581.
    • (1985) J. Biol. Chem. , vol.260 , pp. 1573-1581
    • Pickart, C.M.1    Rose, I.A.2
  • 22
    • 0023682264 scopus 로고
    • Levels of active ubiquitin carrier proteins decline during erythroid maturation
    • Pickart, C. M., and A. T. Vella. 1988. Levels of active ubiquitin carrier proteins decline during erythroid maturation. J. Biol. Chem. 263:12028-12035.
    • (1988) J. Biol. Chem. , vol.263 , pp. 12028-12035
    • Pickart, C.M.1    Vella, A.T.2
  • 23
    • 0024316013 scopus 로고
    • Binding sites of ubiquitin-protein ligase. Binding of ubiquitin-protein conjugates and of ubiquitin-carrier protein
    • Reiss, Y., H. Heller, and A. Hershko. 1989. Binding sites of ubiquitin-protein ligase. Binding of ubiquitin-protein conjugates and of ubiquitin-carrier protein. J. Biol. Chem. 264:10378-10383.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10378-10383
    • Reiss, Y.1    Heller, H.2    Hershko, A.3
  • 24
    • 0028939392 scopus 로고
    • Reconstitution of p53-ubiquitinylation reactions from purified components: The role of human ubiquitin-conjugating enzyme UBC4 and E6-associated protein (E6AP)
    • Rolfe, M., P. Beer-Romero, S. Glass, J. Eckstein, I. Berdo, A. Theodoras, M. Pagano, and G. Draetta. 1995. Reconstitution of p53-ubiquitinylation reactions from purified components: the role of human ubiquitin-conjugating enzyme UBC4 and E6-associated protein (E6AP). Proc. Natl. Acad. Sci. USA 92:3264-3268.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3264-3268
    • Rolfe, M.1    Beer-Romero, P.2    Glass, S.3    Eckstein, J.4    Berdo, I.5    Theodoras, A.6    Pagano, M.7    Draetta, G.8
  • 25
    • 0017225975 scopus 로고
    • Separation of mouse spermatogenic cells by sedimentation velocity
    • Romrell, L. J., A. R. Bellvé, and D. W. Fawcett. 1976. Separation of mouse spermatogenic cells by sedimentation velocity. Dev. Biol. 49:119-131.
    • (1976) Dev. Biol. , vol.49 , pp. 119-131
    • Romrell, L.J.1    Bellvé, A.R.2    Fawcett, D.W.3
  • 26
    • 0017082439 scopus 로고
    • Anchoring device between sertoli cells and late spermatids in rat seminiferous tubules
    • Russell, L., and Y. Clermont. 1976. Anchoring device between sertoli cells and late spermatids in rat seminiferous tubules. Anat. Rec. 185:259-278.
    • (1976) Anat. Rec. , vol.185 , pp. 259-278
    • Russell, L.1    Clermont, Y.2
  • 27
    • 0028607435 scopus 로고
    • Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53
    • Scheffner, M., J. M. Huibregtse, and P. M. Howley. 1994. Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53. Proc. Natl. Acad. Sci. USA 91:8797-8801.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8797-8801
    • Scheffner, M.1    Huibregtse, J.M.2    Howley, P.M.3
  • 28
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
    • Scheffner, M., J. M. Huibregtse, R. D. Vierstra, and P. M. Howley. 1993. The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell 75:495-505.
    • (1993) Cell , vol.75 , pp. 495-505
    • Scheffner, M.1    Huibregtse, J.M.2    Vierstra, R.D.3    Howley, P.M.4
  • 29
    • 0028898424 scopus 로고
    • Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thiolester cascade
    • Scheffner, M., U. Nuber, and J. M. Huibregtse. 1995. Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thiolester cascade. Nature (London) 373:81-83.
    • (1995) Nature (London) , vol.373 , pp. 81-83
    • Scheffner, M.1    Nuber, U.2    Huibregtse, J.M.3
  • 30
    • 0025164762 scopus 로고
    • Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins
    • Seufert, W., and S. Jentsch. 1990. Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins. EMBO J. 9:543-550.
    • (1990) EMBO J. , vol.9 , pp. 543-550
    • Seufert, W.1    Jentsch, S.2
  • 32
    • 0028813764 scopus 로고
    • 17kB) highly expressed in rat testis
    • 17kB) highly expressed in rat testis. Biochem. J. 305:125-132.
    • (1995) Biochem. J. , vol.305 , pp. 125-132
    • Wing, S.1    Jain, P.2


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