메뉴 건너뛰기




Volumn 249, Issue 2, 1997, Pages 427-433

Dynamics of ubiquitin conjugation during heat-shock response revealed by using a monoclonal antibody specific to multi-ubiquitin chains

Author keywords

Heat shock; Histone 2A; Multi ubiquitin chain; Proteasome; Ubiquitin

Indexed keywords

HISTONE H2A; UBIQUITIN;

EID: 0030662038     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00427.x     Document Type: Article
Times cited : (37)

References (46)
  • 2
    • 0028284571 scopus 로고
    • Assisting spontaneity: The role of Hsp90 and small Hsp as molecular chaperones
    • Jakob, U. & Buchner, J. (1994) Assisting spontaneity: the role of Hsp90 and small Hsp as molecular chaperones, Trends Biochem. Sci. 19, 205-211.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 205-211
    • Jakob, U.1    Buchner, J.2
  • 3
    • 0031106824 scopus 로고    scopus 로고
    • Molecular chaperones: Towards a characterization of the heat-shock protein 70 family
    • Rassow, J., von Ahsen, O., Bönier, U. & Pfanner, N. (1997) Molecular chaperones: towards a characterization of the heat-shock protein 70 family, Trends Cell Biol. 7, 129-133.
    • (1997) Trends Cell Biol. , vol.7 , pp. 129-133
    • Rassow, J.1    Von Ahsen, O.2    Bönier, U.3    Pfanner, N.4
  • 6
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser, M. (1996) Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 30, 405-439.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 7
    • 0022000263 scopus 로고
    • Ubiquitin is a heat shock protein in chicken embryo fibroblasts
    • Bond, U. & Schlesinger, M. J. (1985) Ubiquitin is a heat shock protein in chicken embryo fibroblasts, Mol. Cell. Biol. 5, 949-956.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 949-956
    • Bond, U.1    Schlesinger, M.J.2
  • 8
    • 0022999212 scopus 로고
    • The chicken ubiquitin gene contains a heat shock promoter and expresses an unstable mRNA in heat-shocked cells
    • Bond, U. & Schlesinger, M. J. (1986) The chicken ubiquitin gene contains a heat shock promoter and expresses an unstable mRNA in heat-shocked cells, Mol. Cell. Biol. 6, 4602-4610.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 4602-4610
    • Bond, U.1    Schlesinger, M.J.2
  • 10
    • 0023666139 scopus 로고
    • The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses
    • Finley, D., Özkaynak, E. & Varshavsky, A. (1987) The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses, Cell 48, 1035-1046.
    • (1987) Cell , vol.48 , pp. 1035-1046
    • Finley, D.1    Özkaynak, E.2    Varshavsky, A.3
  • 11
    • 0023959560 scopus 로고
    • Dual regulation of the expression of the polyubiquitin gene by cyclic AMP and heat shock in yeast
    • Tanaka, K., Matsumoto, K. & Toh-e, A. (1988) Dual regulation of the expression of the polyubiquitin gene by cyclic AMP and heat shock in yeast. EMBO J. 7, 495-502.
    • (1988) EMBO J. , vol.7 , pp. 495-502
    • Tanaka, K.1    Matsumoto, K.2    Toh-e, A.3
  • 12
    • 0026089183 scopus 로고
    • Cyclin is degraded by the ubiquitin pathway
    • Glotzer, M., Murray, A. W. & Kirschner, M. W. (1991) Cyclin is degraded by the ubiquitin pathway. Nature 349, 132-138.
    • (1991) Nature , vol.349 , pp. 132-138
    • Glotzer, M.1    Murray, A.W.2    Kirschner, M.W.3
  • 13
    • 0027228196 scopus 로고
    • Characterization of DNA synthesis at a restrictive temperature in the temperature-sensitive mutants, tsFT5 cells, that belong to the complementation group of ts85 cells containing a thermolabile ubiquitin-activating enzyme E1
    • 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 mutants, tsFT5 cells, that belong to the complementation group of ts85 cells containing a thermolabile ubiquitin-activating enzyme E1, J. Biol. Chem. 268, 16 803-16 809.
    • (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
  • 14
    • 0023236126 scopus 로고
    • The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme
    • Jentsch, S., McGrath, J. P. & Varshavsky, A. (1987) The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme, Nature 329, 131-134.
    • (1987) Nature , vol.329 , pp. 131-134
    • Jentsch, S.1    McGrath, J.P.2    Varshavsky, A.3
  • 15
    • 0027171066 scopus 로고
    • Ubiquitin pathway involvement in human lymphocyte γ-irradiation-induced apoptosis
    • Delic, J., Morange, M. & Magdelenat, H. (1993) Ubiquitin pathway involvement in human lymphocyte γ-irradiation-induced apoptosis. Mol. Cell. Biol. 13, 4875-4883.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4875-4883
    • Delic, J.1    Morange, M.2    Magdelenat, H.3
  • 17
    • 0026664626 scopus 로고
    • Ligand-induced polyubiquitination of the platelet-derived growth factor β-receptor
    • Mori, S., Heldin, C.-H. & Claesson-Welsh, L. (1992) Ligand-induced polyubiquitination of the platelet-derived growth factor β-receptor, J. Biol. Chem. 267, 6429-6434.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6429-6434
    • Mori, S.1    Heldin, C.-H.2    Claesson-Welsh, L.3
  • 18
    • 0027458572 scopus 로고
    • Cell surface control of the multi-ubiquitination and deubiquitination of high-affinity immunoglobulin E receptors
    • Paolini, R. & Kinet, J.-P. (1993) Cell surface control of the multi-ubiquitination and deubiquitination of high-affinity immunoglobulin E receptors, EMBO J. 12, 779-786.
    • (1993) EMBO J. , vol.12 , pp. 779-786
    • Paolini, R.1    Kinet, J.-P.2
  • 20
    • 0024593537 scopus 로고
    • The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis
    • Finley, D., Bartel, B. & Varshavsky, A. (1989) The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis, Nature 338, 394-401.
    • (1989) Nature , vol.338 , pp. 394-401
    • Finley, D.1    Bartel, B.2    Varshavsky, A.3
  • 21
    • 0024560651 scopus 로고
    • Identification of the long ubiquitin extension as ribosomal protein S27a
    • Redman, K. L. & Rechsteiner, M. (1989) Identification of the long ubiquitin extension as ribosomal protein S27a, Nature 338, 438-440.
    • (1989) Nature , vol.338 , pp. 438-440
    • Redman, K.L.1    Rechsteiner, M.2
  • 22
    • 0027716843 scopus 로고
    • Effects of histone acetylation, ubiquitination and variants on nucleosome stability
    • Li, W., Nagaraja, S., Delcuve, G. P., Hendzel, M. J. & Davie, J. R. (1993) Effects of histone acetylation, ubiquitination and variants on nucleosome stability, Biochem. J. 296, 737-744.
    • (1993) Biochem. J. , vol.296 , pp. 737-744
    • Li, W.1    Nagaraja, S.2    Delcuve, G.P.3    Hendzel, M.J.4    Davie, J.R.5
  • 23
    • 0026782393 scopus 로고
    • The Pas2 protein essential for peroxisome biogenesis is related to ubiquitin-conjugating enzymes
    • Wiebel, F. F. & Kunau, W.-H. (1992) The Pas2 protein essential for peroxisome biogenesis is related to ubiquitin-conjugating enzymes, Nature 359, 73-76.
    • (1992) Nature , vol.359 , pp. 73-76
    • Wiebel, F.F.1    Kunau, W.-H.2
  • 24
    • 0023663064 scopus 로고
    • Arthrin, a myofibrillar protein of insect flight muscle, is an actin-ubiquitin conjugate
    • Ball, E., Karlik, C. C., Beall, C. J., Saville, D. L., Sparrow, J. C., Bullard, B. & Fyrberg, E. A. (1987) Arthrin, a myofibrillar protein of insect flight muscle, is an actin-ubiquitin conjugate, Cell 51, 221-228.
    • (1987) Cell , vol.51 , pp. 221-228
    • Ball, E.1    Karlik, C.C.2    Beall, C.J.3    Saville, D.L.4    Sparrow, J.C.5    Bullard, B.6    Fyrberg, E.A.7
  • 25
    • 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
  • 26
    • 0029870836 scopus 로고    scopus 로고
    • Protein degradation or regulation: Ub the judge
    • Hochstrasser, M . (1996) Protein degradation or regulation: Ub the judge, Cell 84, 813-815.
    • (1996) Cell , vol.84 , pp. 813-815
    • Hochstrasser, M..1
  • 27
    • 0028132691 scopus 로고
    • Proteasomes: Protein degradation machines of the cell
    • Peters, J.-M. (1994) Proteasomes: protein degradation machines of the cell. Trends Biochem. Sci. 19, 377-382.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 377-382
    • Peters, J.-M.1
  • 28
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux, O., Tanaka, K. & Goldberg, A. L. (1996) Structure and functions 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
  • 29
    • 0029867623 scopus 로고    scopus 로고
    • Proteasomes: Destruction as a programme
    • Hilt, W. & Wolf, D. H. (1996) Proteasomes: destruction as a programme, Trends Biochem. Sci. 21, 96-102.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 96-102
    • Hilt, W.1    Wolf, D.H.2
  • 30
    • 0017601447 scopus 로고
    • Isopeptide linkage between nonhistone and histone 2A polypeptides of chromosomal conjugate-protein A24
    • Goldknopf, I. L. & Busch, H. (1977) Isopeptide linkage between nonhistone and histone 2A polypeptides of chromosomal conjugate-protein A24, Proc. Natl Acad. Sci. USA 74, 864-868.
    • (1977) Proc. Natl Acad. Sci. USA , vol.74 , pp. 864-868
    • Goldknopf, I.L.1    Busch, H.2
  • 31
    • 84965822601 scopus 로고
    • Reduced levels of histories H1° and H1h, and unaltered content of methylated DNA in rainbow trout hepatocellular carcinoma chromatin
    • Davie, J. R., Delcuve, G. P., Nickel, B. E., Moirier, R. & Bailey, G. (1987) Reduced levels of histories H1° and H1h, and unaltered content of methylated DNA in rainbow trout hepatocellular carcinoma chromatin, Cancer Res. 47, 5407-5410.
    • (1987) Cancer Res. , vol.47 , pp. 5407-5410
    • Davie, J.R.1    Delcuve, G.P.2    Nickel, B.E.3    Moirier, R.4    Bailey, G.5
  • 32
    • 0024595905 scopus 로고
    • Structure of polyubiquitinated histone H2A
    • Nickel, B. E. & Davie, J. R. (1989) Structure of polyubiquitinated histone H2A, Biochemistry 28, 964-968.
    • (1989) Biochemistry , vol.28 , pp. 964-968
    • Nickel, B.E.1    Davie, J.R.2
  • 33
    • 0021139080 scopus 로고
    • Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85
    • Finley, D., Ciechanover, A. & Varshavsky, A. (1984) Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85, Cell 37, 43-55.
    • (1984) Cell , vol.37 , pp. 43-55
    • Finley, D.1    Ciechanover, A.2    Varshavsky, A.3
  • 34
    • 0023142971 scopus 로고
    • Microinjection of ubiquitin: Changes in protein degradation in HeLa cells subjected to heat-shock
    • Carlson, N., Rogers, S. & Rechsteiner, M (1987) Microinjection of ubiquitin: changes in protein degradation in HeLa cells subjected to heat-shock, J. Cell Biol. 104, 547-555.
    • (1987) J. Cell Biol. , vol.104 , pp. 547-555
    • Carlson, N.1    Rogers, S.2    Rechsteiner, M.3
  • 35
    • 0008585058 scopus 로고
    • Disappearance of a structural chromatin protein A24 in mitosis: Implications for molecular basis of chromatin condensation
    • Matsui, S. I., Seno, B. K. & Sandberg, A. A. (1979) Disappearance of a structural chromatin protein A24 in mitosis: implications for molecular basis of chromatin condensation. Proc. Natl Acad. Sci. USA 76, 6386-6390.
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 6386-6390
    • Matsui, S.I.1    Seno, B.K.2    Sandberg, A.A.3
  • 36
    • 0021140995 scopus 로고
    • Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85
    • Ciechanover, A., Finley, D. & Varshavsky, A. (1984) Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85, Cell 37, 57-66.
    • (1984) Cell , vol.37 , pp. 57-66
    • Ciechanover, A.1    Finley, D.2    Varshavsky, A.3
  • 37
    • 0023087430 scopus 로고
    • Effect of heat shock on protein degradation in mammalian cells: Involvement of the ubiquitin system
    • Parag, H. A., Raboy, B. & Kulka, R. G. (1987) Effect of heat shock on protein degradation in mammalian cells: involvement of the ubiquitin system, EMBO J. 6, 55-61.
    • (1987) EMBO J. , vol.6 , pp. 55-61
    • Parag, H.A.1    Raboy, B.2    Kulka, R.G.3
  • 38
    • 0028070372 scopus 로고
    • Production and characterization of monoclonal antibodies specific to multi-ubiquitin chains of polyubiquitinated proteins
    • Fujimnro, M., Sawada, H. & Yokosawa, H. (1994) Production and characterization of monoclonal antibodies specific to multi-ubiquitin chains of polyubiquitinated proteins, FEBS Lett. 349, 173-180.
    • (1994) FEBS Lett. , vol.349 , pp. 173-180
    • Fujimnro, M.1    Sawada, H.2    Yokosawa, H.3
  • 39
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, 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
    • Laemmli, U.K.1
  • 40
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T. & Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl Acad. Sci. USA 76, 4350-4354.
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 41
    • 0025240329 scopus 로고
    • Radiolabeling of proteins
    • Parker, C. W. (1990) Radiolabeling of proteins, Methods Enzymol. 182, 721-737.
    • (1990) Methods Enzymol. , vol.182 , pp. 721-737
    • Parker, C.W.1
  • 42
    • 0025917982 scopus 로고
    • Improved method for preparation of ubiquitin-ligated lysozyme as substrate of ATP-dependent proteolysis
    • Tamura, T., Tanaka, K., Tanahashi, N. & Ichihara, A. (1991) Improved method for preparation of ubiquitin-ligated lysozyme as substrate of ATP-dependent proteolysis, FEBS Lett. 292, 154-158.
    • (1991) FEBS Lett. , vol.292 , pp. 154-158
    • Tamura, T.1    Tanaka, K.2    Tanahashi, N.3    Ichihara, A.4
  • 43
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 45
    • 0027442427 scopus 로고
    • Different ratios in 20S proteasomes and regulatory subunit complexes in two isoforms of the 26S proteasome purified from rabbit skeletal muscle
    • Sawada, H., Muto, K., Fujimuro, M., Akaishi, T., Takagi Sawada, M., Yokosawa, H. & Goldberg, A. L. (1993) Different ratios in 20S proteasomes and regulatory subunit complexes in two isoforms of the 26S proteasome purified from rabbit skeletal muscle. FEBS Lett. 335, 207-212.
    • (1993) FEBS Lett. , vol.335 , pp. 207-212
    • Sawada, H.1    Muto, K.2    Fujimuro, M.3    Akaishi, T.4    Takagi Sawada, M.5    Yokosawa, H.6    Goldberg, A.L.7
  • 46
    • 0001389495 scopus 로고    scopus 로고
    • Involvement of the molecular chaperone Ydj1 in the ubiquitin-dependent degradation of short-lived and abnormal proteins in Saccharomyces cerevisiae
    • Lee, D. H., Sherman, M. Y. & Goldberg, A. L. (1996) Involvement of the molecular chaperone Ydj1 in the ubiquitin-dependent degradation of short-lived and abnormal proteins in Saccharomyces cerevisiae, Mol. Cell. Biol. 16, 4773-4781.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4773-4781
    • Lee, D.H.1    Sherman, M.Y.2    Goldberg, A.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.