메뉴 건너뛰기




Volumn 101, Issue 1, 1997, Pages 77-85

Ubiquitin conjugation to endogenous proteins in the dormant of Helianthus tuberosus and during the first cell cycle

Author keywords

Cell cycle; Cyclin; Helianthus tuberosus; Jerusalem artichoke; Ubiquitin

Indexed keywords

ADENOSINE TRIPHOSPHATE; CELL CYCLE; DORMANCY; EUKARYOTE; INCUBATION; PLANT GROWTH; PROTEIN DEGRADATION; PROTEIN; REGULATOR PROTEIN; THIOESTER; UBIQUITIN; WESTERN BLOTTING;

EID: 0031394633     PISSN: 00319317     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3054.1997.1010111.x     Document Type: Article
Times cited : (6)

References (45)
  • 1
    • 0030498564 scopus 로고    scopus 로고
    • Ubiquitination and ATP levels in garden pea seeds
    • Agustini, V., McIntosh, T. & Malek, L. 1996. Ubiquitination and ATP levels in garden pea seeds. - Physiol. Plant. 97: 463-468.
    • (1996) Physiol. Plant. , vol.97 , pp. 463-468
    • Agustini, V.1    McIntosh, T.2    Malek, L.3
  • 2
    • 0001186482 scopus 로고
    • Polyamines. storage substances and abscisic acid-like inhibitors during dormancy and very early activation of Helianthus tuberosus tuber tissue
    • Bagni, N., Malucelli, B. & Torrigiani, P. 1980. Polyamines. storage substances and abscisic acid-like inhibitors during dormancy and very early activation of Helianthus tuberosus tuber tissue. - Physiol. Plant. 49: 341-345.
    • (1980) Physiol. Plant. , vol.49 , pp. 341-345
    • Bagni, N.1    Malucelli, B.2    Torrigiani, P.3
  • 3
    • 0346496819 scopus 로고
    • Cell cycle in Helianthus tuberosus tuber tissue in relation to dormancy
    • Bennici, A., Cionini, P. G., Gennai, D. & Cionini, G. 1982. Cell cycle in Helianthus tuberosus tuber tissue in relation to dormancy. - Protoplasma 112: 133-137.
    • (1982) Protoplasma , vol.112 , pp. 133-137
    • Bennici, A.1    Cionini, P.G.2    Gennai, D.3    Cionini, G.4
  • 4
    • 0012589871 scopus 로고
    • Cultivation in vitro of excised pea roots
    • Bonner, J. & Addicott, F. 1937. Cultivation in vitro of excised pea roots. - Bot. Gaz. 99: 144-170.
    • (1937) Bot. Gaz. , vol.99 , pp. 144-170
    • Bonner, J.1    Addicott, F.2
  • 5
    • 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. Biochcm. 72: 248-254.
    • (1976) Anal. Biochcm. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0024514688 scopus 로고
    • A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
    • Chau, V., Tobias, J. V. Baehmair, A., Marriott, D. & Ecker, C. K. 1989. A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. - Science 243: 1576-1583.
    • (1989) Science , vol.243 , pp. 1576-1583
    • Chau, V.1    Tobias, J.V.2    Baehmair, A.3    Marriott, D.4    Ecker, C.K.5
  • 7
    • 0028018268 scopus 로고
    • The ubiquitin-proteasorne proteolytic pathway
    • Ciechanover, A. 1994. The ubiquitin-proteasorne proteolytic pathway.-Cell 79: 13-21.
    • (1994) Cell , vol.79 , pp. 13-21
    • Ciechanover, A.1
  • 8
    • 0006440394 scopus 로고
    • Polyamines and protein modification during the cell cycle
    • J. C. Omrod and D. Francis, eds. Kluwer Academic Publishers. Dordrecht. ISBN 0-7923-1767-X
    • Del Duca, S. & Serafini-Fracassini, D. 1993. Polyamines and protein modification during the cell cycle. - In Molecular and Cell Biology of the Plant Cell Cycle (J. C. Omrod and D. Francis, eds). pp. 143-156. Kluwer Academic Publishers. Dordrecht. ISBN 0-7923-1767-X.
    • (1993) Molecular and Cell Biology of the Plant Cell Cycle , pp. 143-156
    • Del Duca, S.1    Serafini-Fracassini, D.2
  • 9
    • 0028928658 scopus 로고
    • Ubiquitin in the prokaryote Amibaena variabilis
    • Durner, J.& Böger, P. 1995. Ubiquitin in the prokaryote Amibaena variabilis. - J. Biol. Chem. 270: 3720-3725.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3720-3725
    • Durner, J.1    Böger, P.2
  • 10
    • 50549163362 scopus 로고
    • The preparation of two new chromogenic substrates of trypsin
    • Erlanger, B. E., Kokowsky, N. & Cohen, W. 1961. The preparation of two new chromogenic substrates of trypsin. - Arch. Biochem. Biophys. 95: 271-278.
    • (1961) Arch. Biochem. Biophys. , vol.95 , pp. 271-278
    • Erlanger, B.E.1    Kokowsky, N.2    Cohen, W.3
  • 11
    • 0012621311 scopus 로고
    • Ultrastructure and uutoradiography of dormant and activated parenchyma of Helianthus tuberosus
    • Favali, M. A., Serafini-Fracassini, D. & Sartorato, P. 1984. Ultrastructure and uutoradiography of dormant and activated parenchyma of Helianthus tuberosus. - Protoplasma 123: 192-202.
    • (1984) Protoplasma , vol.123 , pp. 192-202
    • Favali, M.A.1    Serafini-Fracassini, D.2    Sartorato, P.3
  • 12
    • 0022971584 scopus 로고
    • Tranter RNA is required for conjugation of uhiquitin to selective substrates of the uhiquitin- And ATP-dependent proteolytic system
    • Ferber, S. & Ciechanover, A. 1986. Tranter RNA is required for conjugation of uhiquitin to selective substrates of the uhiquitin- and ATP-dependent proteolytic system. - J. Biol. Chem. 261: 3128-3134.
    • (1986) J. Biol. Chem. , vol.261 , pp. 3128-3134
    • Ferber, S.1    Ciechanover, A.2
  • 13
  • 15
    • 0026089183 scopus 로고
    • Cyclin is degraded by the ubiquilin pathway
    • Glotzer, M., Murray, A. & Kirschner M. W. 1991. Cyclin is degraded by the ubiquilin pathway. - Nature 349: 132-138.
    • (1991) Nature , vol.349 , pp. 132-138
    • Glotzer, M.1    Murray, A.2    Kirschner, M.W.3
  • 16
    • 0022379602 scopus 로고
    • The immunochemical detection and quantitalion of intracellular Ub-protein conjugates
    • Haas, A. L. & Bright, P. M. 1985. The immunochemical detection and quantitalion of intracellular Ub-protein conjugates. -J. Biol.Chem. 260: 12464-12473.
    • (1985) J. Biol.Chem. , vol.260 , pp. 12464-12473
    • Haas, A.L.1    Bright, P.M.2
  • 17
    • 0023802469 scopus 로고
    • The resolution and characterization of putative ubiquitin carrier protein isozymes from rabbit reticulocytes
    • _ & 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
    • Bright, P.M.1
  • 18
    • 0020478717 scopus 로고
    • Ubiquitin activating enzyme: Mechanism and role in uhiquitin-protein conjugation
    • _ , Warms, J. V. B., Hershko, A. & Rose, I. A. 1982. Ubiquitin activating enzyme: Mechanism and role in uhiquitin-protein conjugation. - J. Biol. Chem. 257: 2543-2548.
    • (1982) J. Biol. Chem. , vol.257 , pp. 2543-2548
    • Warms, J.V.B.1    Hershko, A.2    Rose, I.A.3
  • 19
    • 0025605089 scopus 로고
    • Ubiquitin-mediated degradation of histone H3 does not require the substrate-binding ubiquitin protein liguse. E3, or attachment of polyubiquitin chains
    • _ . Reback, P. M., Pratt, G. & Rechsteiner, M. 1990. Ubiquitin-mediated degradation of histone H3 does not require the substrate-binding ubiquitin protein liguse. E3, or attachment of polyubiquitin chains. - J. Biol. Chem. 265: 21664-21669.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21664-21669
    • Reback, P.M.1    Pratt, G.2    Rechsteiner, M.3
  • 20
    • 38249042340 scopus 로고
    • Ubiquitination of cell surface glycoproteins
    • Hart, G. W. 1986. Ubiquitination of cell surface glycoproteins. Trends Biochem. Sci. 11: 272.
    • (1986) Trends Biochem. Sci. , vol.11 , pp. 272
    • Hart, G.W.1
  • 21
    • 0000334676 scopus 로고
    • Ubiquitin-dependent proteolytic pathway in wheat germ: Isolation of multiple forms of ubiquilin-activating enzyme
    • Hatfield, P. M. & Vierstra, R. D. 1989. Ubiquitin-dependent proteolytic pathway in wheat germ: Isolation of multiple forms of ubiquilin-activating enzyme. E1. - Biochemistry 28: 735-742,
    • (1989) El. - Biochemistry , vol.28 , pp. 735-742
    • Hatfield, P.M.1    Vierstra, R.D.2
  • 22
    • 0023768491 scopus 로고
    • Ubiquitin-mediated protein degradation
    • Hershko, A. 1988. Ubiquitin-mediated protein degradation. - J. Biol. Chem. 263: 15237-15240.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15237-15240
    • Hershko, A.1
  • 23
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • _ & Ciechanover, A. 1992. The ubiquitin system for protein degradation. - Annu. Rev. Biochem. 61: 761-807.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 761-807
    • Ciechanover, A.1
  • 24
    • 0021813071 scopus 로고
    • Occurrence of a polyubiquitin structure in ubiquitin-protein conjugates
    • _ & Heller, A. 1985. Occurrence of a polyubiquitin structure in ubiquitin-protein conjugates. - Biochem. Biophys. Res. Commun. 128: 1079-1086.
    • (1985) Biochem. Biophys. Res. Commun. , vol.128 , pp. 1079-1086
    • Heller, A.1
  • 25
    • 0022967107 scopus 로고
    • Ubiquitin-lysozyme conjugates
    • Hough, R. & Rechsteiner, M. 1986. Ubiquitin-lysozyme conjugates. - J. Biol. Chem. 261: 2391-2399.
    • (1986) J. Biol. Chem. , vol.261 , pp. 2391-2399
    • Hough, R.1    Rechsteiner, M.2
  • 27
    • 0023236126 scopus 로고
    • The DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme
    • Jentseh, S., Me Grath, J. P. & Varshavsky, A. 1987. The DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme. - Nature 329: 131-134.
    • (1987) Nature , vol.329 , pp. 131-134
    • Jentseh, S.1    Me Grath, J.P.2    Varshavsky, A.3
  • 29
    • 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
  • 31
    • 0029051233 scopus 로고
    • Cyclin ubiquitination: The destructive end of mitosis
    • Murray, A. 1995. Cyclin ubiquitination: The destructive end of mitosis.-Cell 81: 149-152.
    • (1995) Cell , vol.81 , pp. 149-152
    • Murray, A.1
  • 32
    • 0029000579 scopus 로고
    • Cyclins and cyclin-dependent kinases: A biochemical view
    • Pines, J. 1995. Cyclins and cyclin-dependent kinases: A biochemical view. - Biochem. J. 308: 697-711.
    • (1995) Biochem. J. , vol.308 , pp. 697-711
    • Pines, J.1
  • 33
    • 0001782253 scopus 로고
    • The ubiquitin system in higher and lower plants - Pathways in protein metabolism
    • Pollmann, L. & Wettern, M. 1989. The ubiquitin system in higher and lower plants - pathways in protein metabolism. Bot. Acta 102: 21-30.
    • (1989) Bot. Acta , vol.102 , pp. 21-30
    • Pollmann, L.1    Wettern, M.2
  • 34
    • 0028239065 scopus 로고
    • Cloning of four cyclins from maize indicates that higher plants have three structurally distinct groups of milotic cyclins
    • Renaudin, J. P., Colasanti, J., Rime, H., Yuan, Z. & Sundaresan. V. 1994. Cloning of four cyclins from maize indicates that higher plants have three structurally distinct groups of milotic cyclins. - Proc. Natl. Acad. Sci. USA 91: 7.175-7379.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7175-7379
    • Renaudin, J.P.1    Colasanti, J.2    Rime, H.3    Yuan, Z.4    Sundaresan, V.5
  • 35
    • 0006203790 scopus 로고
    • Cell cycle-dependent changes in plant polyamine metabolism
    • R. D. Slocum and H. E. Flores, eds, CRC Press, Boca Raton, KL. ISBN 0-8493-6865-0
    • Serafini-Fracassini, D. 1991. Cell cycle-dependent changes in plant polyamine metabolism. - In Biochemistry and Physiology of Polyamines in Plants (R. D. Slocum and H. E. Flores, eds), pp. 159-173. CRC Press, Boca Raton, KL. ISBN 0-8493-6865-0.
    • (1991) Biochemistry and Physiology of Polyamines in Plants , pp. 159-173
    • Serafini-Fracassini, D.1
  • 36
    • 0012617106 scopus 로고
    • Polyamines and nucleic acids during the first cell cycle of Helianthus tuberosus tissue after the dormancy break
    • _ , Bagni, N., Cionini, P. G. & Bennici, A. 1980. Polyamines and nucleic acids during the first cell cycle of Helianthus tuberosus tissue after the dormancy break. - Planta 148: 332-337.
    • (1980) Planta , vol.148 , pp. 332-337
    • Bagni, N.1    Cionini, P.G.2    Bennici, A.3
  • 37
    • 0023154514 scopus 로고
    • Red light-induced formation of uhiquitin-phytochrome conjugates: Identification of possible intermediates of phytochrome degradation
    • Shanklin, J., Jabben, M. & Vierstra, R. D. 1987. Red light-induced formation of uhiquitin-phytochrome conjugates: Identification of possible intermediates of phytochrome degradation. - Proc. Natl. Acad. Sci. USA 84: 359-363.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 359-363
    • Shanklin, J.1    Jabben, M.2    Vierstra, R.D.3
  • 38
    • 0002943340 scopus 로고
    • Heal shock induced change in protein ubiquilination in Chlamydomonas
    • Shimogawara, K & Muto, S. 1989. Heal shock induced change in protein ubiquilination in Chlamydomonas. - Plant Cell Physiol. 30: 9-16.
    • (1989) Plant Cell Physiol. , vol.30 , pp. 9-16
    • Shimogawara, K.1    Muto, S.2
  • 39
    • 0006418264 scopus 로고
    • High performance liquid Chromatography resolution of ubiquitin pathway enzymes from wheat germ
    • Sullivan, M. L., Callis, J. & Vierstra, R. D. 1990. High performance liquid Chromatography resolution of ubiquitin pathway enzymes from wheat germ. - Plant Physiol. 94: 710-716.
    • (1990) Plant Physiol. , vol.94 , pp. 710-716
    • Sullivan, M.L.1    Callis, J.2    Vierstra, R.D.3
  • 40
    • 2642607567 scopus 로고
    • Early DNA synthesis and polyamines in mitochondria from activated parenchyma of Helianthus tuberosus
    • Torrigiani, P. & Serafini-Fraeassini, D. 1980. Early DNA synthesis and polyamines in mitochondria from activated parenchyma of Helianthus tuberosus. - Z. Pflanzenphysiol. 97: 353-359.
    • (1980) Z. Pflanzenphysiol. , vol.97 , pp. 353-359
    • Torrigiani, P.1    Serafini-Fraeassini, D.2
  • 41
    • 0000774315 scopus 로고
    • Polyamine biosynthesis and effect of dicyclohexylamine during the cell cycle of Heliamthus tuberous tuber
    • _ , Scrafini-Fracassini, D. & Bagni, N. 1987. Polyamine biosynthesis and effect of dicyclohexylamine during the cell cycle of Heliamthus tuberous tuber. - Plant Physiol. 84: 148-152.
    • (1987) Plant Physiol. , vol.84 , pp. 148-152
    • Scrafini-Fracassini, D.1    Bagni, N.2
  • 42
    • 84897584811 scopus 로고
    • Diamine oxidase activity in different physiological stages of Helianthus tuberosus tuber
    • _ . Serafini-Fracassini, D. & Fara, A. 1989. Diamine oxidase activity in different physiological stages of Helianthus tuberosus tuber. - Plant Physiol. 89: 69-73.
    • (1989) Plant Physiol. , vol.89 , pp. 69-73
    • Serafini-Fracassini, D.1    Fara, A.2
  • 43
    • 0009482260 scopus 로고
    • Eleclrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T. & Gordon, J. 1979. Eleclrophoretic 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
  • 45
    • 0344361158 scopus 로고
    • Growth and differentiation of plant tissue culture. II. Synchronous cell division in developing callus cultures
    • Yeoman, M. M. & Evans, P. K. 1967. Growth and differentiation of plant tissue culture. II. Synchronous cell division in developing callus cultures. - Ann. Bot. 31: 323-332.
    • (1967) Ann. Bot. , vol.31 , pp. 323-332
    • Yeoman, M.M.1    Evans, P.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.