메뉴 건너뛰기




Volumn 199, Issue 1, 1996, Pages 139-151

Subcellular localization of ubiquitin in plant protoplasts and the function of ubiquitin in selective degradation of outer-wall plasmodesmata in regenerating protoplasts

Author keywords

Immunolocalization; Plasmodesmata degradation (outer cell wall); Protoplast culture; Solanum; Ubiquitin; Vicia

Indexed keywords

ANIMALIA; PHASEOLUS (ANGIOSPERM); SOLANUM; SOLANUM NIGRUM; VICIA; VICIA FABA;

EID: 0000099522     PISSN: 00320935     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF00196890     Document Type: Article
Times cited : (28)

References (47)
  • 1
    • 0028254541 scopus 로고
    • Ultrastructural specializations of the cell wall sleeve around plasmodesmata
    • Badelt K, White RG, Overall RL, Vesk M (1994) Ultrastructural specializations of the cell wall sleeve around plasmodesmata. Amer J Bot 81: 1422-1427
    • (1994) Amer J Bot , vol.81 , pp. 1422-1427
    • Badelt, K.1    White, R.G.2    Overall, R.L.3    Vesk, M.4
  • 2
    • 84989737710 scopus 로고
    • Current perspectives on plasmodesmata: Structure and function
    • Beebe DU, Turgeon R (1991) Current perspectives on plasmodesmata: structure and function. Physiol Plant 83: 194-199
    • (1991) Physiol Plant , vol.83 , pp. 194-199
    • Beebe, D.U.1    Turgeon, R.2
  • 3
    • 0002887043 scopus 로고
    • Haploid Solanum dulcamara L: Shoot culture and plant regeneration from isolated protoplasts
    • Binding H, Mordhorst G (1984) Haploid Solanum dulcamara L: Shoot culture and plant regeneration from isolated protoplasts. Plant Sci Lett 35: 77-79
    • (1984) Plant Sci Lett , vol.35 , pp. 77-79
    • Binding, H.1    Mordhorst, G.2
  • 4
    • 0001121964 scopus 로고
    • Regeneration of isolated protoplasts to plants in Solanum dulcamara L
    • Binding H, Nehls R (1977) Regeneration of isolated protoplasts to plants in Solanum dulcamara L. Z Pflanzenphysiol 85: 279-280
    • (1977) Z Pflanzenphysiol , vol.85 , pp. 279-280
    • Binding, H.1    Nehls, R.2
  • 5
    • 0002955593 scopus 로고
    • Plant cell graft chimeras obtained by co-culture of isolated protoplasts
    • Binding H, Witt D, Monzer J, Mordhorst G, Kollmann R (1987) Plant cell graft chimeras obtained by co-culture of isolated protoplasts. Protoplasma 141: 64-73
    • (1987) Protoplasma , vol.141 , pp. 64-73
    • Binding, H.1    Witt, D.2    Monzer, J.3    Mordhorst, G.4    Kollmann, R.5
  • 7
    • 0027950823 scopus 로고
    • Plasmodesmal-mediated cell-to-cell transport in wheat roots is modulated by anaerobic stress
    • Cleland RE, Fujiwara T, Lucas WJ (1994) Plasmodesmal-mediated cell-to-cell transport in wheat roots is modulated by anaerobic stress. Protoplasma 178: 81-85
    • (1994) Protoplasma , vol.178 , pp. 81-85
    • Cleland, R.E.1    Fujiwara, T.2    Lucas, W.J.3
  • 8
    • 0002469966 scopus 로고
    • Substructure of freeze-substituted plasmodesmata
    • Ding B, Turgeon R, Parthasarathy MV (1992) Substructure of freeze-substituted plasmodesmata. Protoplasma 169: 28-41
    • (1992) Protoplasma , vol.169 , pp. 28-41
    • Ding, B.1    Turgeon, R.2    Parthasarathy, M.V.3
  • 9
    • 0002499801 scopus 로고
    • Formation of branched plasmodesmata in regenerating Solanum nigrum-protoplasts
    • Ehlers K, Kollmann R (1995) Formation of branched plasmodesmata in regenerating Solanum nigrum-protoplasts. Planta 199: 126-138
    • (1995) Planta , vol.199 , pp. 126-138
    • Ehlers, K.1    Kollmann, R.2
  • 11
    • 0024593537 scopus 로고
    • The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosomes biogenesis
    • Finley D, Bartel B, Varshavsky A (1989) The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosomes biogenesis. Nature 338: 394-401
    • (1989) Nature , vol.338 , pp. 394-401
    • Finley, D.1    Bartel, B.2    Varshavsky, A.3
  • 13
    • 0346864044 scopus 로고
    • In vivo localization of ubiquitin in tobacco mosaic virus infected and uninfected tobacco cells
    • Gaspar JO, Dunigan DD, Zaitlin IM (1990) In vivo localization of ubiquitin in tobacco mosaic virus infected and uninfected tobacco cells. Mol Plant-Microbe Interact 3: 182-187
    • (1990) Mol Plant-Microbe Interact , vol.3 , pp. 182-187
    • Gaspar, J.O.1    Dunigan, D.D.2    Zaitlin, I.M.3
  • 14
    • 0000177006 scopus 로고
    • Mise en évidence de la résistance aux triazines chez Solanum nigrum L. et Polygonum lapathifolium L. par observation de la fluorescence des feuilles isolées
    • Gasquez J, Barralis G (1979) Mise en évidence de la résistance aux triazines chez Solanum nigrum L. et Polygonum lapathifolium L. par observation de la fluorescence des feuilles isolées. CR Acad Sci (Paris) Sec D 288: 1391-1393
    • (1979) CR Acad Sci (Paris) Sec D , vol.288 , pp. 1391-1393
    • Gasquez, J.1    Barralis, G.2
  • 15
    • 5244256107 scopus 로고
    • Isopeptide linkage between non-histone and histone 2A polypeptides of chromosomal conjugate protein A24
    • Goldkopf IL, Busch H (1975) Isopeptide linkage between non-histone and histone 2A polypeptides of chromosomal conjugate protein A24. Proc Natl Acad Sci USA 72: 11-15
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 11-15
    • Goldkopf, I.L.1    Busch, H.2
  • 16
    • 0028136693 scopus 로고
    • Protein synthesis elongation factor EF-1a is essential for ubiquitin dependent degradation of certain N-acetylated proteins and may be substituted for the bacterial elongation factor EF-TU
    • Gonen H, Smith CE, Siegel NR, Kahana C, Merrick WC, Chakraburtty K, Schwartz AL, Ciechanover A (1994) Protein synthesis elongation factor EF-1a is essential for ubiquitin dependent degradation of certain N-acetylated proteins and may be substituted for the bacterial elongation factor EF-TU. Proc Natl Acad Sci USA 91: 7648-7652
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 7648-7652
    • Gonen, H.1    Smith, C.E.2    Siegel, N.R.3    Kahana, C.4    Merrick, W.C.5    Chakraburtty, K.6    Schwartz, A.L.7    Ciechanover, A.8
  • 17
    • 0020479850 scopus 로고
    • Immunochemical analyses of the turnover of ubiquitin protein conjugates in intact cells
    • Hershko A, Eytan E, Ciechanover A, Haas AL (1982) Immunochemical analyses of the turnover of ubiquitin protein conjugates in intact cells. J Biol Chem 257: 13964-13970
    • (1982) J Biol Chem , vol.257 , pp. 13964-13970
    • Hershko, A.1    Eytan, E.2    Ciechanover, A.3    Haas, A.L.4
  • 18
    • 0026409423 scopus 로고
    • Isolation and characterization of tomato cDNA and genomic clones encoding the ubiquitin gene ubi3
    • Hoffman NE, Ko K, Milkowski D, Pichersky E (1991) Isolation and characterization of tomato cDNA and genomic clones encoding the ubiquitin gene ubi3. Plant Mol Biol 17: 1189-1201
    • (1991) Plant Mol Biol , vol.17 , pp. 1189-1201
    • Hoffman, N.E.1    Ko, K.2    Milkowski, D.3    Pichersky, E.4
  • 20
    • 0028300216 scopus 로고
    • Cloning and characterization of two ubiquitin: 76-amino acid extension protein-encoding fusion genes from Lupinus albus
    • Jacinto A, Neves NM, Vassilevskaia TD, Ricardo CP, Rodrigues-Pousada C (1994) Cloning and characterization of two ubiquitin: 76-amino acid extension protein-encoding fusion genes from Lupinus albus. Gene 139: 201-205
    • (1994) Gene , vol.139 , pp. 201-205
    • Jacinto, A.1    Neves, N.M.2    Vassilevskaia, T.D.3    Ricardo, C.P.4    Rodrigues-Pousada, C.5
  • 21
    • 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
  • 22
    • 33847765193 scopus 로고
    • Studies on graft unions. I. Plasmodesmata between cells of plants belonging to different unrelated taxa
    • Kollmann R, Glockmann C (1985) Studies on graft unions. I. Plasmodesmata between cells of plants belonging to different unrelated taxa. Protoplasma 124: 224-235
    • (1985) Protoplasma , vol.124 , pp. 224-235
    • Kollmann, R.1    Glockmann, C.2
  • 23
    • 33847752459 scopus 로고
    • Studies on graft unions. III. On the mechanism of secondary formation of plasmodesmata at the graft interface
    • Kollmann R, Glockmann C (1991) Studies on graft unions. III. On the mechanism of secondary formation of plasmodesmata at the graft interface. Protoplasma 165: 71-85
    • (1991) Protoplasma , vol.165 , pp. 71-85
    • Kollmann, R.1    Glockmann, C.2
  • 24
    • 0027498124 scopus 로고
    • Immunogold localization of ubiquitin protein conjugates in Sf9 insect cells
    • Löw P, Doherty FJ, Sass M, Kovacs J, Mayer RJ, Laszlo L (1993) Immunogold localization of ubiquitin protein conjugates in Sf9 insect cells. FEBS Lett 316: 152-156
    • (1993) FEBS Lett , vol.316 , pp. 152-156
    • Löw, P.1    Doherty, F.J.2    Sass, M.3    Kovacs, J.4    Mayer, R.J.5    Laszlo, L.6
  • 25
    • 0027145372 scopus 로고
    • Plasmodesmata and the supracellular nature of plants
    • Lucas WJ, Ding B, Van der Schoot C (1993) Plasmodesmata and the supracellular nature of plants. New Phytol 125: 435-476
    • (1993) New Phytol , vol.125 , pp. 435-476
    • Lucas, W.J.1    Ding, B.2    Van Der Schoot, C.3
  • 26
    • 0025718671 scopus 로고
    • Evidence for a particulate location of ubiquitin conjugates and ubiquitin conjugating enzymes in rabbit brain
    • Magnani M, Serafini G, Antonelli A, Malatesta M, Gazzanelli G (1991) Evidence for a particulate location of ubiquitin conjugates and ubiquitin conjugating enzymes in rabbit brain. J Biol Chem 266: 21018-21024
    • (1991) J Biol Chem , vol.266 , pp. 21018-21024
    • Magnani, M.1    Serafini, G.2    Antonelli, A.3    Malatesta, M.4    Gazzanelli, G.5
  • 28
    • 0005207759 scopus 로고
    • Secondary formation of plasmodesmala in cultured cells - Structural and functional aspects
    • Robards AW, Jongsma H, Lucas WJ, Pitts J, Spray D (eds) Parallels in cell to cell junctions in plants and animals Springer, Berlin Heidelberg New York Tokyo
    • Monzer J (1990) Secondary formation of plasmodesmala in cultured cells - structural and functional aspects. In: Robards AW, Jongsma H, Lucas WJ, Pitts J, Spray D (eds) Parallels in cell to cell junctions in plants and animals (NATO ASI Series, Vol H 46). Springer, Berlin Heidelberg New York Tokyo, pp 185-197
    • (1990) NATO ASI Series , vol.H 46 , pp. 185-197
    • Monzer, J.1
  • 29
    • 0003377144 scopus 로고
    • Ultrastructure of secondary plasmodesmata formation in regenerating Solanum nigrum-protoplast cultures
    • Monzer J (1991) Ultrastructure of secondary plasmodesmata formation in regenerating Solanum nigrum-protoplast cultures. Protoplasma 165: 86-95
    • (1991) Protoplasma , vol.165 , pp. 86-95
    • Monzer, J.1
  • 31
    • 0023913829 scopus 로고
    • Ubiquitin is a component of the microtubule network
    • Murti G, Smith HT, Fried UA (1988) Ubiquitin is a component of the microtubule network. Proc Natl Acad Sci USA 85: 3019-3023
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 3019-3023
    • Murti, G.1    Smith, H.T.2    Fried, U.A.3
  • 32
    • 0001918456 scopus 로고
    • The neck region of plasmodesmata: General architecture and some functional aspects
    • Robards AW, Jongsma H, Lucas WJ, Pitts J, Spray D (eds) Parallels in cell to cell junctions in plants and animals Springer, Berlin Heidelberg New York Tokyo
    • Olesen P, Robards AW (1990) The neck region of plasmodesmata: general architecture and some functional aspects. In: Robards AW, Jongsma H, Lucas WJ, Pitts J, Spray D (eds) Parallels in cell to cell junctions in plants and animals (NATO ASI Series, Vol H 46). Springer, Berlin Heidelberg New York Tokyo, pp 145-170
    • (1990) NATO ASI Series , vol.H 46 , pp. 145-170
    • Olesen, P.1    Robards, A.W.2
  • 33
    • 0028234770 scopus 로고
    • Distinct 19S and 20S subcomplexes of the 26S proteasome and their distribution in the nucleus and the cytoplasm
    • Peters JM, Frank WW, Kleinschmidt JA (1994) Distinct 19S and 20S subcomplexes of the 26S proteasome and their distribution in the nucleus and the cytoplasm. J Biol Chem 269: 7709-7718
    • (1994) J Biol Chem , vol.269 , pp. 7709-7718
    • Peters, J.M.1    Frank, W.W.2    Kleinschmidt, J.A.3
  • 35
    • 0028830802 scopus 로고
    • Plasmodesmal widening accompanies the short-term increase in symplasmic phloem unloading of pea root tips under osmotic stress
    • Schulz A (1995) Plasmodesmal widening accompanies the short-term increase in symplasmic phloem unloading of pea root tips under osmotic stress. Protoplasma 188: 22-37
    • (1995) Protoplasma , vol.188 , pp. 22-37
    • Schulz, A.1
  • 36
    • 84995013253 scopus 로고
    • Immunofluorescent localization of a connexin 26-like protein at the surface of mesophyll protoplasts from Vicia faba L. and Helianthus annuus L
    • Schulz M, Traub O, Knop M, Willecke K, Schnabl H (1992a) Immunofluorescent localization of a connexin 26-like protein at the surface of mesophyll protoplasts from Vicia faba L. and Helianthus annuus L. Bot Acta 105: 111-115
    • (1992) Bot Acta , vol.105 , pp. 111-115
    • Schulz, M.1    Traub, O.2    Knop, M.3    Willecke, K.4    Schnabl, H.5
  • 37
    • 5244315121 scopus 로고
    • Age dependent appearance of polypeptides with immunoreactivity to ubiquitin antibodies in chloroplast membranes of Vicia faba L
    • Schulz M, Wolf D, Schnabl H (1992b) Age dependent appearance of polypeptides with immunoreactivity to ubiquitin antibodies in chloroplast membranes of Vicia faba L. J Plant Physiol 141: 298-303
    • (1992) J Plant Physiol , vol.141 , pp. 298-303
    • Schulz, M.1    Wolf, D.2    Schnabl, H.3
  • 38
    • 0028103172 scopus 로고
    • Stress and age related spots with immunoreactivity to ubiquitin antibody at protoplast surfaces
    • Schulz M, Janßen M, Knop M, Schnabl H (1994) Stress and age related spots with immunoreactivity to ubiquitin antibody at protoplast surfaces. Plant Cell Physiol 35: 551-556
    • (1994) Plant Cell Physiol , vol.35 , pp. 551-556
    • Schulz, M.1    Janßen, M.2    Knop, M.3    Schnabl, H.4
  • 39
    • 0026664253 scopus 로고
    • Immunoelectron microscopic localization of the ubiquitin-activating enzyme E1 in HepG2 cells
    • Schwartz AL, Trausch JS, Ciechanover A, Slot JW, Geuze H (1992) Immunoelectron 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
    • Schwartz, A.L.1    Trausch, J.S.2    Ciechanover, A.3    Slot, J.W.4    Geuze, H.5
  • 40
    • 0023154514 scopus 로고
    • Red light mediated formation of ubiquitin-phytochrome conjugates. Identification of possible intermediates of phytochrome degradation
    • Shanklin J, Jabben M, Vierstra RD (1987) Red light mediated formation of ubiquitin-phytochrome conjugates. Identification of possible intermediates of phytochrome degradation. Proc Natl Acad Sci USA 84: 359-365
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 359-365
    • Shanklin, J.1    Jabben, M.2    Vierstra, R.D.3
  • 41
    • 0027327659 scopus 로고
    • A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum
    • Sommer T, Jentsch S (1993) A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum. Nature 365: 176-179
    • (1993) Nature , vol.365 , pp. 176-179
    • Sommer, T.1    Jentsch, S.2
  • 42
    • 0000186886 scopus 로고
    • Intracellular localization of phytochrome and ubiquitin in red light-irradiated coleoptiles by electron microscopy
    • Speth V, Otto V, Schäfer E (1987) Intracellular localization of phytochrome and ubiquitin in red light-irradiated coleoptiles by electron microscopy. Planta 171: 332-338
    • (1987) Planta , vol.171 , pp. 332-338
    • Speth, V.1    Otto, V.2    Schäfer, E.3
  • 43
    • 5244344403 scopus 로고
    • Identification of ubiquitinated histones and their changes during the cell cycle in synchronous cultures of Catharanthus roseus cells
    • Tagami T, Kodama H, Komamine A (1993) Identification of ubiquitinated histones and their changes during the cell cycle in synchronous cultures of Catharanthus roseus cells. Plant Physiol (Life Sci Adv) 12: 45-51
    • (1993) Plant Physiol (Life Sci Adv) , vol.12 , pp. 45-51
    • Tagami, T.1    Kodama, H.2    Komamine, A.3
  • 44
    • 84986932392 scopus 로고
    • Ubiquitin, a key component in the degradation of plant protein
    • Vierstra RD (1987) Ubiquitin, a key component in the degradation of plant protein. Physiol Plant 70: 103-106
    • (1987) Physiol Plant , vol.70 , pp. 103-106
    • Vierstra, R.D.1
  • 45
    • 0025046096 scopus 로고
    • Ubiquitin in Chlamydomonas reinhardtii. Distribution in the cell and effect of heatshock and photoinhibition on its conjugate pattern
    • Wettern M, Parag HA, Pollmann L, Ohad I, Kulka RG (1990) Ubiquitin in Chlamydomonas reinhardtii. Distribution in the cell and effect of heatshock and photoinhibition on its conjugate pattern. Eur J Biochem 191: 571-576
    • (1990) Eur J Biochem , vol.191 , pp. 571-576
    • Wettern, M.1    Parag, H.A.2    Pollmann, L.3    Ohad, I.4    Kulka, R.G.5
  • 47
    • 0027213027 scopus 로고
    • Ubiquitin found in the archaebacterium Thermoplasma acidophilum
    • Wolf S, Lottspeich F, Baumeister W (1993) Ubiquitin found in the archaebacterium Thermoplasma acidophilum. FEBS Lett 326: 42-44
    • (1993) FEBS Lett , vol.326 , pp. 42-44
    • Wolf, S.1    Lottspeich, F.2    Baumeister, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.