메뉴 건너뛰기




Volumn 48, Issue 10-11, 2010, Pages 808-812

SDS-dependent proteases induced by ABA and its relation to Rubisco and Rubisco activase contents in rice leaves

Author keywords

Abscisic acid; Protease; Rice; Rubisco; Rubisco activase; SDS; Senescence

Indexed keywords

ABSCISIC ACID; ADENINE; CYCLOHEXIMIDE; PEPTIDE HYDROLASE; RCA PROTEIN, PLANT; RIBULOSEBISPHOSPHATE CARBOXYLASE; VEGETABLE PROTEIN;

EID: 77958162431     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2010.08.002     Document Type: Article
Times cited : (19)

References (32)
  • 1
    • 77957184339 scopus 로고
    • Change in the amounts of Ribulose bisphosphate carboxylase synthesized and degraded during the life span of rice leaf (Oryza sativa L.)
    • Mae T., Makino A., Ohira K. Change in the amounts of Ribulose bisphosphate carboxylase synthesized and degraded during the life span of rice leaf (Oryza sativa L.). Plant Cell Physiol. 1983, 24:1079-1086.
    • (1983) Plant Cell Physiol. , vol.24 , pp. 1079-1086
    • Mae, T.1    Makino, A.2    Ohira, K.3
  • 2
    • 0030468542 scopus 로고    scopus 로고
    • Relationships between photosynthetic activity and the amounts of Rubisco activase and Rubisco in rice leaves from emergence through senescence
    • Fukayama H., Uchida N., Azuma T., Yasuda T. Relationships between photosynthetic activity and the amounts of Rubisco activase and Rubisco in rice leaves from emergence through senescence. Jpn. J. Crop. Sci. 1996, 65:296-302.
    • (1996) Jpn. J. Crop. Sci. , vol.65 , pp. 296-302
    • Fukayama, H.1    Uchida, N.2    Azuma, T.3    Yasuda, T.4
  • 3
    • 0000663317 scopus 로고
    • Changes in photosynthetic capacity in rice leaves from emergence through senescence. Analysis from ribulose-1,5-bisphosphate carboxylase and leaf conductance
    • Makino A., Mae T., Ohira K. Changes in photosynthetic capacity in rice leaves from emergence through senescence. Analysis from ribulose-1,5-bisphosphate carboxylase and leaf conductance. Plant Cell Physiol. 1984, 25:511-521.
    • (1984) Plant Cell Physiol. , vol.25 , pp. 511-521
    • Makino, A.1    Mae, T.2    Ohira, K.3
  • 4
    • 44649135348 scopus 로고    scopus 로고
    • Regulation of Rubisco activase and its interaction with Rubisco
    • Portis A.R., Li C., Wang D., Salvucci M.E. Regulation of Rubisco activase and its interaction with Rubisco. J. Exp. Bot. 2008, 59:1597-1604.
    • (2008) J. Exp. Bot. , vol.59 , pp. 1597-1604
    • Portis, A.R.1    Li, C.2    Wang, D.3    Salvucci, M.E.4
  • 5
    • 0031401470 scopus 로고    scopus 로고
    • Ribulose-1,5-bisphosphate carboxylase/oxygenase activase deficiency delays senescence of ribulose-1,5-bisphosphate carboxylase/oxygenase but progressively impairs its catalysis during tobacco leaf development
    • He Z., von Caemmerer S., Hudson G.S., Price G.D., Badger M.R., Andrews T.J. Ribulose-1,5-bisphosphate carboxylase/oxygenase activase deficiency delays senescence of ribulose-1,5-bisphosphate carboxylase/oxygenase but progressively impairs its catalysis during tobacco leaf development. Plant Physiol. 1997, 115:1569-1580.
    • (1997) Plant Physiol. , vol.115 , pp. 1569-1580
    • He, Z.1    von Caemmerer, S.2    Hudson, G.S.3    Price, G.D.4    Badger, M.R.5    Andrews, T.J.6
  • 6
    • 33646263110 scopus 로고    scopus 로고
    • Antisense inhibition of Rubisco activase increases Rubisco content and alters the proportion of Rubisco activase in stroma and thylakoids in chloroplasts of rice leaves
    • Jin S.-H., Hong J., Li X.-Q., Jiang D.-A. Antisense inhibition of Rubisco activase increases Rubisco content and alters the proportion of Rubisco activase in stroma and thylakoids in chloroplasts of rice leaves. Ann. Bot. 2006, 97:739-744.
    • (2006) Ann. Bot. , vol.97 , pp. 739-744
    • Jin, S.-H.1    Hong, J.2    Li, X.-Q.3    Jiang, D.-A.4
  • 8
    • 47649129736 scopus 로고    scopus 로고
    • Senescence-associated degradation of chloroplast proteins inside and outside the organelle
    • Martínez D.E., Costa M.L., Guiamet J.J. Senescence-associated degradation of chloroplast proteins inside and outside the organelle. Plant Biol. 2008, 10:15-22.
    • (2008) Plant Biol. , vol.10 , pp. 15-22
    • Martínez, D.E.1    Costa, M.L.2    Guiamet, J.J.3
  • 9
    • 0036857415 scopus 로고    scopus 로고
    • The degradation of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase into the 44-kDa fragment in the lysates of chloroplasts incubated in darkness
    • Kokubun N., Ishida H., Makino A., Mae T. The degradation of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase into the 44-kDa fragment in the lysates of chloroplasts incubated in darkness. Plant Cell Physiol. 2008, 43:1390-1395.
    • (2008) Plant Cell Physiol. , vol.43 , pp. 1390-1395
    • Kokubun, N.1    Ishida, H.2    Makino, A.3    Mae, T.4
  • 10
    • 34547737969 scopus 로고    scopus 로고
    • A novel 51-kDa fragment of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase formed in the stroma of chloroplasts in dark-induced senescing wheat leaves
    • Zhang L.F., Rui Q., Zhang P., Wang X.Y., Xu L.L. A novel 51-kDa fragment of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase formed in the stroma of chloroplasts in dark-induced senescing wheat leaves. Physiol. Plant 2007, 131:64-71.
    • (2007) Physiol. Plant , vol.131 , pp. 64-71
    • Zhang, L.F.1    Rui, Q.2    Zhang, P.3    Wang, X.Y.4    Xu, L.L.5
  • 11
    • 44649118756 scopus 로고    scopus 로고
    • Rubiscolytics: fate of Rubisco after its enzymatic function in a cell is terminated
    • Feller U., Anders I., Mae T. Rubiscolytics: fate of Rubisco after its enzymatic function in a cell is terminated. J. Exp. Bot. 2008, 59:1615-1624.
    • (2008) J. Exp. Bot. , vol.59 , pp. 1615-1624
    • Feller, U.1    Anders, I.2    Mae, T.3
  • 12
    • 0347297276 scopus 로고    scopus 로고
    • Abscisic acid and cytokinins in the root exudates and leaves and their relationship to senescence and remobilization of carbon reserves in rice subjected to water stress during grain filling
    • Yang J., Zhang J., Wang Z., Zhu Q., Liu L. Abscisic acid and cytokinins in the root exudates and leaves and their relationship to senescence and remobilization of carbon reserves in rice subjected to water stress during grain filling. Planta 2002, 215:645-652.
    • (2002) Planta , vol.215 , pp. 645-652
    • Yang, J.1    Zhang, J.2    Wang, Z.3    Zhu, Q.4    Liu, L.5
  • 13
    • 0000164781 scopus 로고
    • Neutral peptidases in stroma of pea chloroplast
    • Liu X.-Q., Jagendorf A.T. Neutral peptidases in stroma of pea chloroplast. Plant Physiol. 1986, 81:603-608.
    • (1986) Plant Physiol. , vol.81 , pp. 603-608
    • Liu, X.-Q.1    Jagendorf, A.T.2
  • 14
    • 0027141619 scopus 로고
    • A purified zinc protease of pea chloroplasts, EP1, degrades the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase
    • Bushnell T.P., Bushnell B., Jagendolf A.T. A purified zinc protease of pea chloroplasts, EP1, degrades the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase. Plant Physiol. 1993, 103:585-591.
    • (1993) Plant Physiol. , vol.103 , pp. 585-591
    • Bushnell, T.P.1    Bushnell, B.2    Jagendolf, A.T.3
  • 15
    • 0030452596 scopus 로고    scopus 로고
    • Coordination of protein and mRNA abundance of stromal enzymes and mRNA abundance of the Clp protease subunits during senescence of Phaseolus vulgalis (L) leaves
    • Crafts-Brandner S.J., Klein R.R., Klein P., Horzer R., Feller U. Coordination of protein and mRNA abundance of stromal enzymes and mRNA abundance of the Clp protease subunits during senescence of Phaseolus vulgalis (L) leaves. Planta 1996, 200:312-318.
    • (1996) Planta , vol.200 , pp. 312-318
    • Crafts-Brandner, S.J.1    Klein, R.R.2    Klein, P.3    Horzer, R.4    Feller, U.5
  • 16
    • 0001040455 scopus 로고
    • Newly synthesized proteins are degraded by an ATP-stimulated proteolytic process in isolated pea chloroplasts
    • Malek L., Bogorad L., Ayers A.R., Goldberg A.L. Newly synthesized proteins are degraded by an ATP-stimulated proteolytic process in isolated pea chloroplasts. FEBS Lett. 1984, 166:253-257.
    • (1984) FEBS Lett. , vol.166 , pp. 253-257
    • Malek, L.1    Bogorad, L.2    Ayers, A.R.3    Goldberg, A.L.4
  • 17
    • 0027976015 scopus 로고
    • Hydroxyl radicals and a thylakoid-bond endopeptidase are involved in light-and oxygen-induced proteolysis in oat chloroplasts
    • Casano L.M., Lascano H.R., Trippi V.S. Hydroxyl radicals and a thylakoid-bond endopeptidase are involved in light-and oxygen-induced proteolysis in oat chloroplasts. Plant Cell Physiol. 1994, 35:145-152.
    • (1994) Plant Cell Physiol. , vol.35 , pp. 145-152
    • Casano, L.M.1    Lascano, H.R.2    Trippi, V.S.3
  • 18
    • 0025183394 scopus 로고
    • Increased susceptibility of Ribulose-1,5-bisphosphate carboxylase/oxygenase to proteolytic degradation caused by oxidative treatment
    • Penarrubia L., Moreno J. Increased susceptibility of Ribulose-1,5-bisphosphate carboxylase/oxygenase to proteolytic degradation caused by oxidative treatment. Arch. Biochem. Biophys. 1990, 281:319-323.
    • (1990) Arch. Biochem. Biophys. , vol.281 , pp. 319-323
    • Penarrubia, L.1    Moreno, J.2
  • 19
    • 0000938347 scopus 로고
    • Characteristics of ribulose-1,5-bisphosphate carboxylase/oxygenase degradation by lysates of mechanically isolated chloroplasts from wheat leaves
    • Miyadai K., Mae T., Makino A., Ojima K. Characteristics of ribulose-1,5-bisphosphate carboxylase/oxygenase degradation by lysates of mechanically isolated chloroplasts from wheat leaves. Plant Physiol. 1990, 92:1215-1219.
    • (1990) Plant Physiol. , vol.92 , pp. 1215-1219
    • Miyadai, K.1    Mae, T.2    Makino, A.3    Ojima, K.4
  • 20
    • 0028078197 scopus 로고
    • Two mechanisms of recovery from photoinhibition in vivo: reactivation of photosystem II related and unrelated to D1 turnover
    • Leitsch J., Schnrttger B., Critchley C., Krause G.H. Two mechanisms of recovery from photoinhibition in vivo: reactivation of photosystem II related and unrelated to D1 turnover. Planta 1994, 194:15-21.
    • (1994) Planta , vol.194 , pp. 15-21
    • Leitsch, J.1    Schnrttger, B.2    Critchley, C.3    Krause, G.H.4
  • 21
    • 0033166098 scopus 로고    scopus 로고
    • Molecular characterization of ribulose-1,5-bisphosphate carboxylase/oxygenase activase in rice leaves
    • To K.-Y., Suen D.-F., Chen S.C.G. Molecular characterization of ribulose-1,5-bisphosphate carboxylase/oxygenase activase in rice leaves. Planta 1999, 209:66-76.
    • (1999) Planta , vol.209 , pp. 66-76
    • To, K.-Y.1    Suen, D.-F.2    Chen, S.C.G.3
  • 22
    • 55549117167 scopus 로고    scopus 로고
    • Mobilization of rubisco and stroma-localized fluorescent proteins of chloroplasts to the vacuole by an ATG gene-dependent autophagic process
    • Ishida H., Yoshimoto K., Izumi M., Reisen D., Yano Y., Makino A., Ohsumi Y., Hanson M.R., Mae T. Mobilization of rubisco and stroma-localized fluorescent proteins of chloroplasts to the vacuole by an ATG gene-dependent autophagic process. Plant Physiol. 2009, 148:142-155.
    • (2009) Plant Physiol. , vol.148 , pp. 142-155
    • Ishida, H.1    Yoshimoto, K.2    Izumi, M.3    Reisen, D.4    Yano, Y.5    Makino, A.6    Ohsumi, Y.7    Hanson, M.R.8    Mae, T.9
  • 23
    • 77957185897 scopus 로고
    • Degradation of ribulose-1,5-bisphosphate carboxylase/oxygenase in the lysates of the chloroplasts isolated mechanically from wheat (Triticum aestivum L.) leaves
    • Mae T., Kamei C., Funaki K., Miyadai K., Makino A., Ohira K., Ojima K. Degradation of ribulose-1,5-bisphosphate carboxylase/oxygenase in the lysates of the chloroplasts isolated mechanically from wheat (Triticum aestivum L.) leaves. Plant Cell Physiol. 1989, 30:193-200.
    • (1989) Plant Cell Physiol. , vol.30 , pp. 193-200
    • Mae, T.1    Kamei, C.2    Funaki, K.3    Miyadai, K.4    Makino, A.5    Ohira, K.6    Ojima, K.7
  • 25
    • 57649171450 scopus 로고    scopus 로고
    • Characterization and cloning of cysteine protease that is induced in green leaves of barley, Plant Sci.
    • Y. Watanabe, S. Matsushima, A. Yamaguchi, Y. Shioi, Characterization and cloning of cysteine protease that is induced in green leaves of barley, Plant Sci., 176: 264-271.
    • , vol.176 , pp. 264-271
    • Watanabe, Y.1    Matsushima, S.2    Yamaguchi, A.3    Shioi, Y.4
  • 26
    • 0026794712 scopus 로고
    • Purification and initial characterization of the proteasome from the higher plant Spinacia oleracea
    • Ozaki M., Fujinami K., Tanaka K., Amemiya Y., Sato T., Ogura N., Nakagawa H. Purification and initial characterization of the proteasome from the higher plant Spinacia oleracea. J. Biol. Chem. 1992, 267:21678-21684.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21678-21684
    • Ozaki, M.1    Fujinami, K.2    Tanaka, K.3    Amemiya, Y.4    Sato, T.5    Ogura, N.6    Nakagawa, H.7
  • 27
    • 0033166888 scopus 로고    scopus 로고
    • Vacuolar processing enzyme is up-regulated in the lytic vacuoles of vegetative tissues during senescence and under various stressed conditions
    • Kinoshita T., Yamada K., Hiraiwa N., Kondo M., Nishimura M., Hara-Nishimura I. Vacuolar processing enzyme is up-regulated in the lytic vacuoles of vegetative tissues during senescence and under various stressed conditions. Plant J. 1999, 19:43-53.
    • (1999) Plant J. , vol.19 , pp. 43-53
    • Kinoshita, T.1    Yamada, K.2    Hiraiwa, N.3    Kondo, M.4    Nishimura, M.5    Hara-Nishimura, I.6
  • 28
    • 34247186321 scopus 로고    scopus 로고
    • Vacuolar cysteine proteases of wheat (Triticum aestivum L.) are common to leaf senescence induced by different factors
    • Martínez D.E., Bartoli C.G., Grbic V., Guiamet J.J. Vacuolar cysteine proteases of wheat (Triticum aestivum L.) are common to leaf senescence induced by different factors. J. Exp. Bot. 2007, 58:1099-1107.
    • (2007) J. Exp. Bot. , vol.58 , pp. 1099-1107
    • Martínez, D.E.1    Bartoli, C.G.2    Grbic, V.3    Guiamet, J.J.4
  • 29
    • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 30
    • 0018854046 scopus 로고
    • Electrophoretic analysis of plasminogen activators in polyacrylamide gel containing sodium dodecyl sulfate and copolymerized substrate
    • Heussen C., Dowdle E.B. Electrophoretic analysis of plasminogen activators in polyacrylamide gel containing sodium dodecyl sulfate and copolymerized substrate. Anal. Biochem. 1980, 102:196-202.
    • (1980) Anal. Biochem. , vol.102 , pp. 196-202
    • Heussen, C.1    Dowdle, E.B.2
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature 1970, 277:608-685.
    • (1970) Nature , vol.277 , pp. 608-685
    • Laemmli, U.K.1
  • 32
    • 0023664635 scopus 로고
    • Sequence from picomole quantities protein electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira P. Sequence from picomole quantities protein electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 1987, 262:10035-10038.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.