메뉴 건너뛰기




Volumn 48, Issue 314, 1997, Pages 1639-1645

Requirements for the light-stimulated degradation of stromal proteins in isolated pea (Pisum sativum L.) chloroplasts

Author keywords

Isolated pea chloroplasts; Light induced protein degradation

Indexed keywords

PISUM SATIVUM; SATIVUM;

EID: 0030687928     PISSN: 00220957     EISSN: None     Source Type: Journal    
DOI: 10.1093/jxb/48.9.1639     Document Type: Article
Times cited : (27)

References (44)
  • 1
    • 0027199986 scopus 로고
    • Photoinhibition of photosystem II. Inactivation, protein damage and turnover
    • Aro E-M, Virgin I, Andersson B. 1993. Photoinhibition of photosystem II. Inactivation, protein damage and turnover. Biochimica et Biophysica Acta 1143, 113-34.
    • (1993) Biochimica et Biophysica Acta , vol.1143 , pp. 113-134
    • Aro, E.-M.1    Virgin, I.2    Andersson, B.3
  • 2
    • 0026785393 scopus 로고
    • Tentoxin sensitivity of chloroplasts determined by codon 83 of β subunit of proton-ATPase
    • Avni A, Anderson JD, Holland N, Rochaix J-D, Gromet-Elhanan Z, Edelman M. 1992. Tentoxin sensitivity of chloroplasts determined by codon 83 of β subunit of proton-ATPase. Science 257, 1245-7.
    • (1992) Science , vol.257 , pp. 1245-1247
    • Avni, A.1    Anderson, J.D.2    Holland, N.3    Rochaix, J.-D.4    Gromet-Elhanan, Z.5    Edelman, M.6
  • 3
    • 1842360660 scopus 로고
    • Light-induced electric potentials of intact Anthoceros chloroplasts and their modification in the presence of the energy transfer inhibitor tentoxin
    • Bulychev AA, Dahse I. 1984. Light-induced electric potentials of intact Anthoceros chloroplasts and their modification in the presence of the energy transfer inhibitor tentoxin. Biochemie und Physiologie der Pflanzen 179, 685-92.
    • (1984) Biochemie und Physiologie der Pflanzen , vol.179 , pp. 685-692
    • Bulychev, A.A.1    Dahse, I.2
  • 4
    • 0027141619 scopus 로고
    • A purified zinc protease of pea chloroplasts, EP1, degrades the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase
    • Bushnell TP, Bushnell D, Jagendorf AT. 1993. A purified zinc protease of pea chloroplasts, EP1, degrades the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase. Plant Physiology 103, 585-91.
    • (1993) Plant Physiology , vol.103 , pp. 585-591
    • Bushnell, T.P.1    Bushnell, D.2    Jagendorf, A.T.3
  • 5
    • 0028814328 scopus 로고
    • Regulation of protein degradation
    • Callis J. 1995. Regulation of protein degradation. The Plant Cell 7, 845-57.
    • (1995) The Plant Cell , vol.7 , pp. 845-857
    • Callis, J.1
  • 6
    • 0039297341 scopus 로고
    • Oxygen- and light-induced proteolysis in isolated oat chloroplasts
    • Casano LM, Gomez LD, Trippi VS. 1990. Oxygen-and light-induced proteolysis in isolated oat chloroplasts. Plant and Cell Physiology 31, 377-82.
    • (1990) Plant and Cell Physiology , vol.31 , pp. 377-382
    • Casano, L.M.1    Gomez, L.D.2    Trippi, V.S.3
  • 7
    • 0000908246 scopus 로고
    • The effect of oxygen radicals on proteolysis in isolated oat chloroplasts
    • Casano LM, Trippi VS. 1992. The effect of oxygen radicals on proteolysis in isolated oat chloroplasts. Plant and Cell Physiology 33, 329-32.
    • (1992) Plant and Cell Physiology , vol.33 , pp. 329-332
    • Casano, L.M.1    Trippi, V.S.2
  • 8
    • 0000205390 scopus 로고
    • Inactivation of ascorbate peroxidase by thiols requires hydrogen peroxide
    • Chen G-X, Asada K. 1992. Inactivation of ascorbate peroxidase by thiols requires hydrogen peroxide. Plant and Cell Physiology 33, 117-23.
    • (1992) Plant and Cell Physiology , vol.33 , pp. 117-123
    • Chen, G.-X.1    Asada, K.2
  • 9
    • 1842358704 scopus 로고
    • A compansion of tentoxin action on the delayed fluorescence in chloroplasts of spinach, Chlorella and Anacystis
    • Dahse I, Matorin DN, Liebermann B. 1986. A compansion of tentoxin action on the delayed fluorescence in chloroplasts of spinach, Chlorella and Anacystis. Biochemie und Physiologie der Pflanzen 181, 137-46.
    • (1986) Biochemie und Physiologie der Pflanzen , vol.181 , pp. 137-146
    • Dahse, I.1    Matorin, D.N.2    Liebermann, B.3
  • 10
    • 0001165153 scopus 로고    scopus 로고
    • Oxidative stress induces partial degradation of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase in isolated chloroplasts of barley
    • Desimone M, Henke A, Wagner E. 1996. Oxidative stress induces partial degradation of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase in isolated chloroplasts of barley. Plant Physiology 111, 789-96.
    • (1996) Plant Physiology , vol.111 , pp. 789-796
    • Desimone, M.1    Henke, A.2    Wagner, E.3
  • 11
    • 0017862062 scopus 로고
    • Production of hydrogen peroxide by photosystem II of spinach chloroplast lamellae
    • Elstner EF, Frommeyer D. 1978. Production of hydrogen peroxide by photosystem II of spinach chloroplast lamellae. FEBS Letters 86, 143-6.
    • (1978) FEBS Letters , vol.86 , pp. 143-146
    • Elstner, E.F.1    Frommeyer, D.2
  • 12
    • 0028155031 scopus 로고
    • Oxidative modification and breakdown of ribulose-1,5-bisphosphate carboxylase/ oxygenase inuced in Euglena gracilis
    • Garcia-Ferris C, Moreno J. 1994. Oxidative modification and breakdown of ribulose-1,5-bisphosphate carboxylase/ oxygenase inuced in Euglena gracilis. Planta 193, 208-15.
    • (1994) Planta , vol.193 , pp. 208-215
    • Garcia-Ferris, C.1    Moreno, J.2
  • 13
    • 0028953463 scopus 로고
    • Xanthophyll cycle-dependent quenching of photosystem II chlorophyll a fluorescence: Formation of a quenching complex with a short fluorescence lifetime
    • Gilmore AM, Hazlett T, Govindjee. 1995. Xanthophyll cycle-dependent quenching of photosystem II chlorophyll a fluorescence: formation of a quenching complex with a short fluorescence lifetime. Proceedings of the National Academy of Science, USA 92, 2273-7.
    • (1995) Proceedings of the National Academy of Science, USA , vol.92 , pp. 2273-2277
    • Gilmore, A.M.1    Hazlett, T.2    Govindjee3
  • 14
    • 0026503828 scopus 로고
    • The mechanism and functions of ATP-dependent proteases in bacterial and animal cells
    • Goldberg AL. 1992. The mechanism and functions of ATP-dependent proteases in bacterial and animal cells. European Journal of Biochemistry 203, 9-23.
    • (1992) European Journal of Biochemistry , vol.203 , pp. 9-23
    • Goldberg, A.L.1
  • 16
    • 0028010460 scopus 로고
    • Protein catabolism in bean leaf discs: Accumulation of a soluble fragment of ribulose-1,5-bisphosphate carboxylase/oxygenase under oxygen deficiency
    • Hildbrand M, Fischer A, Feller U. 1994. Protein catabolism in bean leaf discs: accumulation of a soluble fragment of ribulose-1,5-bisphosphate carboxylase/oxygenase under oxygen deficiency. Journal of Experimental Botany 45, 1197-1204.
    • (1994) Journal of Experimental Botany , vol.45 , pp. 1197-1204
    • Hildbrand, M.1    Fischer, A.2    Feller, U.3
  • 17
    • 0028395591 scopus 로고
    • Nucleotide sequence of a Brassica napus Clp homolog
    • Ko K, Doung C, Ko ZW. 1994. Nucleotide sequence of a Brassica napus Clp homolog. Plant Physiology 104, 1087-9.
    • (1994) Plant Physiology , vol.104 , pp. 1087-1089
    • Ko, K.1    Doung, C.2    Ko, Z.W.3
  • 18
    • 0001141978 scopus 로고
    • The biochemical basis for photoinhibition of photosystem II
    • Kyle DJ, Osmond CB, Arntzen CJ, eds. Amsterdam: Elsevier
    • Kyle DJ. 1987. The biochemical basis for photoinhibition of photosystem II. In: Kyle DJ, Osmond CB, Arntzen CJ, eds. Photoinhibition. Amsterdam: Elsevier, 197-227.
    • (1987) Photoinhibition , pp. 197-227
    • Kyle, D.J.1
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0029034534 scopus 로고
    • Regulatory proteolysis of the major light-harvesting chlorophyll a/b protein of photosystem II by a light-induced membrane-associated enzymic system
    • Lindahl M, Yang D-H, Andersson B. 1995. Regulatory proteolysis of the major light-harvesting chlorophyll a/b protein of photosystem II by a light-induced membrane-associated enzymic system. European Journal of Biochemistry 231, 503-9.
    • (1995) European Journal of Biochemistry , vol.231 , pp. 503-509
    • Lindahl, M.1    Yang, D.-H.2    Andersson, B.3
  • 22
    • 48749135011 scopus 로고
    • ATP-dependent proteolysis in pea chloroplasts
    • Liu X-Q, Jagendorf AT. 1984. ATP-dependent proteolysis in pea chloroplasts. FEBS Letters 166, 248-52.
    • (1984) FEBS Letters , vol.166 , pp. 248-252
    • Liu, X.-Q.1    Jagendorf, A.T.2
  • 23
    • 0343031435 scopus 로고
    • Roles for ATP-dependent and ATP-independent proteases of pea chloroplasts in regulation of the plastid translation products
    • Liu X-Q, Jagendorf AT. 1985. Roles for ATP-dependent and ATP-independent proteases of pea chloroplasts in regulation of the plastid translation products. Physiologie Végétale 23, 749-55.
    • (1985) Physiologie Végétale , vol.23 , pp. 749-755
    • Liu, X.-Q.1    Jagendorf, A.T.2
  • 24
    • 0000164781 scopus 로고
    • Neutral peptidases in the stroma of pea chloroplasts
    • Liu X-Q, Jagendorf AT. 1986. Neutral peptidases in the stroma of pea chloroplasts. Plant Physiology 81, 603-8.
    • (1986) Plant Physiology , vol.81 , pp. 603-608
    • Liu, X.-Q.1    Jagendorf, A.T.2
  • 25
    • 12044258108 scopus 로고
    • Effects of nitrogen nutrition on nitrogen partitioning between chloroplasts and mitochondria in pea and wheat
    • Makino A, Osmond B. 1991. Effects of nitrogen nutrition on nitrogen partitioning between chloroplasts and mitochondria in pea and wheat. Plant Physiology 96, 355-62.
    • (1991) Plant Physiology , vol.96 , pp. 355-362
    • Makino, A.1    Osmond, B.2
  • 26
    • 0001040455 scopus 로고
    • Newly synthesised proteins are degraded by an ATP-stimulated proteolytic process in isolated pea chloroplasts
    • Malek L, Bogorad L, Ayers AR, Goldberg AL. 1984. Newly synthesised proteins are degraded by an ATP-stimulated proteolytic process in isolated pea chloroplasts. FEBS Letters 166, 253-7.
    • (1984) FEBS Letters , vol.166 , pp. 253-257
    • Malek, L.1    Bogorad, L.2    Ayers, A.R.3    Goldberg, A.L.4
  • 27
    • 0001294420 scopus 로고
    • Regulation of protein metabolism: Coupling of photosynthetic electron transport to in vivo degradation of the rapidly metabolized 32-kilodalton protein of the chloroplast membranes
    • Mattoo AK, Hoffman-Falk H, Marder JB, Edelman M. 1984. Regulation of protein metabolism: coupling of photosynthetic electron transport to in vivo degradation of the rapidly metabolized 32-kilodalton protein of the chloroplast membranes. Proceedings of the National Academy of Science, USA 81, 1380-4.
    • (1984) Proceedings of the National Academy of Science, USA , vol.81 , pp. 1380-1384
    • Mattoo, A.K.1    Hoffman-Falk, H.2    Marder, J.B.3    Edelman, M.4
  • 28
    • 0026601663 scopus 로고
    • Proteases and protein degradation in Escherichia coli
    • Maurizi MR. 1992. Proteases and protein degradation in Escherichia coli. Experientia 48, 178-201.
    • (1992) Experientia , vol.48 , pp. 178-201
    • Maurizi, M.R.1
  • 30
    • 0026795063 scopus 로고
    • Oxidative stress causes rapid membrane translocation and in vivo degradation of ribulose-1,5-bisphosphate carboxylase oxygenase
    • Mehta RA, Fawcett TW, Porath D, Mattoo AK. 1992. Oxidative stress causes rapid membrane translocation and in vivo degradation of ribulose-1,5-bisphosphate carboxylase oxygenase. Journal of Biological Chemistry 267, 2810-16.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 2810-2816
    • Mehta, R.A.1    Fawcett, T.W.2    Porath, D.3    Mattoo, A.K.4
  • 31
    • 23044485253 scopus 로고
    • Ribulose-1,5-bisphosphate carboxylase/oxygenase degradation in isolated pea chloroplasts incubated in the light or in the dark
    • Mitsuhashi W, Crafts-Brandner SJ, Feller U. 1992. Ribulose-1,5-bisphosphate carboxylase/oxygenase degradation in isolated pea chloroplasts incubated in the light or in the dark Journal of Plant Physiology 139, 653-8.
    • (1992) Journal of Plant Physiology , vol.139 , pp. 653-658
    • Mitsuhashi, W.1    Crafts-Brandner, S.J.2    Feller, U.3
  • 32
    • 0000712047 scopus 로고
    • Effects of light and external solutes on the catabolism of nuclear-encoded stromal proteins in intact chloroplasts isolated from pea leaves
    • Mitsuhashi W, Feller U. 1992. Effects of light and external solutes on the catabolism of nuclear-encoded stromal proteins in intact chloroplasts isolated from pea leaves. Plant Physiology 100, 2100-5.
    • (1992) Plant Physiology , vol.100 , pp. 2100-2105
    • Mitsuhashi, W.1    Feller, U.2
  • 33
    • 0027550578 scopus 로고
    • Characterization of a cDNA clone encoding a chloroplast-targeted Clp homologue
    • Moore T, Keegstra K. 1993. Characterization of a cDNA clone encoding a chloroplast-targeted Clp homologue. Plant Molecular Biology 21, 525-37.
    • (1993) Plant Molecular Biology , vol.21 , pp. 525-537
    • Moore, T.1    Keegstra, K.2
  • 34
    • 0030248598 scopus 로고    scopus 로고
    • The iron-catalyzed oxidation of dithiothreitol is a biphasic process: Hydrogen peroxide is involved in the initiation of a free radical chain of reactions
    • Netto LES, Stadtman ER. 1996. The iron-catalyzed oxidation of dithiothreitol is a biphasic process: hydrogen peroxide is involved in the initiation of a free radical chain of reactions. Archives of Biochemistry and Biophysics 333, 233-42.
    • (1996) Archives of Biochemistry and Biophysics , vol.333 , pp. 233-242
    • Netto, L.E.S.1    Stadtman, E.R.2
  • 35
    • 0027140766 scopus 로고
    • Multiple effects of dithiothreitol on non-photochemical fluorescence quenching in intact chloroplasts
    • Neubauer C. 1993. Multiple effects of dithiothreitol on non-photochemical fluorescence quenching in intact chloroplasts. Plant Physiology 103, 575-83.
    • (1993) Plant Physiology , vol.103 , pp. 575-583
    • Neubauer, C.1
  • 37
    • 0000434458 scopus 로고
    • Differential changes in the synthesis and steady-state levels of thylakoid proteins during bean leaf senescence
    • Roberts DR, Thompson JE, Dumbroff EB, Gepstein S, Mattoo AK. 1987. Differential changes in the synthesis and steady-state levels of thylakoid proteins during bean leaf senescence. Plant Molecular Biology 9, 343-53.
    • (1987) Plant Molecular Biology , vol.9 , pp. 343-353
    • Roberts, D.R.1    Thompson, J.E.2    Dumbroff, E.B.3    Gepstein, S.4    Mattoo, A.K.5
  • 38
    • 0029392885 scopus 로고
    • The stroma of higher plant plastids contain ClpP and ClpC, functional homologs of Escherichia coli ClpP and ClpA: An archetypal two-component ATP-dependent protease
    • Shanklin J, DeWitt ND, Flanagan JM. 1995. The stroma of higher plant plastids contain ClpP and ClpC, functional homologs of Escherichia coli ClpP and ClpA: an archetypal two-component ATP-dependent protease. The Plant Cell 7, 1713-22.
    • (1995) The Plant Cell , vol.7 , pp. 1713-1722
    • Shanklin, J.1    DeWitt, N.D.2    Flanagan, J.M.3
  • 39
    • 0026795635 scopus 로고
    • Protein oxidation and aging
    • Stadtman ER. 1992. Protein oxidation and aging. Science 257, 1220-4.
    • (1992) Science , vol.257 , pp. 1220-1224
    • Stadtman, E.R.1
  • 40
    • 0342597234 scopus 로고
    • Influence of external factors on the catabolism of stromal proteins in isolated pea chloroplasts
    • Mathis P, ed. Dordrecht: Kluwer Academic Publishes
    • Stieger PA, Feller U. 1995. Influence of external factors on the catabolism of stromal proteins in isolated pea chloroplasts. In: Mathis P, ed. Photosynthesis: from light to biosphere. Dordrecht: Kluwer Academic Publishes, 223-6.
    • (1995) Photosynthesis: From Light to Biosphere , pp. 223-226
    • Stieger, P.A.1    Feller, U.2
  • 42
    • 0024278052 scopus 로고
    • Organization of the oxygen-evolution enzyme complex studied by butanol/water phase partitioning of spinach photosystem II
    • Yamamoto Y. 1988. Organization of the oxygen-evolution enzyme complex studied by butanol/water phase partitioning of spinach photosystem II. Journal of Biological Chemistry 263, 497-500.
    • (1988) Journal of Biological Chemistry , vol.263 , pp. 497-500
    • Yamamoto, Y.1
  • 43
    • 0029115182 scopus 로고
    • Degradation of antenna chlorophyll-binding protein CP43 during photoinhibition of photosystem II
    • Yamamoto Y, Akasaka T. 1995. Degradation of antenna chlorophyll-binding protein CP43 during photoinhibition of photosystem II. Biochemistry 34, 9038-45.
    • (1995) Biochemistry , vol.34 , pp. 9038-9045
    • Yamamoto, Y.1    Akasaka, T.2
  • 44
    • 0015520731 scopus 로고
    • The effects of dithiothreitol on violaxanthin de-epoxidation and absorbance changes in the 500 nm region
    • Yamamoto H, Kamite L. 1972. The effects of dithiothreitol on violaxanthin de-epoxidation and absorbance changes in the 500 nm region. Biochimica et Biophysica Acta 267, 538-43.
    • (1972) Biochimica et Biophysica Acta , vol.267 , pp. 538-543
    • Yamamoto, H.1    Kamite, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.