메뉴 건너뛰기




Volumn 258, Issue 1-2, 1998, Pages 166-173

Mutagenesis of the genes encoding subunits A, C, H, I, J and K of the plastid NAD(P)H-plastoquinone-oxidoreductase in tobacco by polyethylene glycol-mediated plastome transformation

Author keywords

Chlororespiration; Complex I; NAD(P)H plastoquinone oxidoreductase; Nicotiana tabacum; Plastid transformation

Indexed keywords

CHLOROPHYLL; DNA; MACROGOL; OXIDOREDUCTASE; PLASTOQUINONE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE); STARCH;

EID: 0031948338     PISSN: 00268925     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004380050719     Document Type: Article
Times cited : (148)

References (38)
  • 1
    • 0029934521 scopus 로고    scopus 로고
    • Deletion of rpoB reveals a second distinct transcription system in plastids of higher plants
    • Allison LA, Simon LD, Maliga P (1996) Deletion of rpoB reveals a second distinct transcription system in plastids of higher plants. EMBO J 15:2802-2809
    • (1996) EMBO J , vol.15 , pp. 2802-2809
    • Allison, L.A.1    Simon, L.D.2    Maliga, P.3
  • 2
    • 0000796565 scopus 로고
    • 6 f complex: Dynamic molecular organization, function and acclimation
    • 6 f complex: dynamic molecular organization, function and acclimation. Photosynth Res 34:341-357
    • (1992) Photosynth Res , vol.34 , pp. 341-357
    • Andersen, J.M.1
  • 3
    • 0000305538 scopus 로고
    • The organization of glycolysis and the oxidative pentose phosphate pathway in plants
    • Douce R, Day DA (eds) Springer-Verlag, Berlin-New York
    • Ap Rees T (1985) The organization of glycolysis and the oxidative pentose phosphate pathway in plants. In: Douce R, Day DA (eds) Encyclopedia of Physiology (New Series), vol 18. Springer-Verlag, Berlin-New York, pp 391-417
    • (1985) Encyclopedia of Physiology (New Series) , vol.18 , pp. 391-417
    • Ap Rees, T.1
  • 4
    • 0001844190 scopus 로고
    • Copper enzymes in isolated chloroplasts. Polyphenoloxidase in Beta vulgaris
    • Arnon DI (1949) Copper enzymes in isolated chloroplasts. Polyphenoloxidase in Beta vulgaris. Plant Physiol 21:1-13
    • (1949) Plant Physiol , vol.21 , pp. 1-13
    • Arnon, D.I.1
  • 5
    • 0023359272 scopus 로고
    • Why do chloroplasts and mitochondria contain so many copies of their genome?
    • Bendich AJ (1987) Why do chloroplasts and mitochondria contain so many copies of their genome? BioEssays 6:279-282
    • (1987) BioEssays , vol.6 , pp. 279-282
    • Bendich, A.J.1
  • 6
    • 0000454893 scopus 로고
    • Evidence for a respiratory chain in the chloroplast
    • Bennoun P (1982) Evidence for a respiratory chain in the chloroplast. Proc Natl Acad Sci USA 79:4342-4356
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 4342-4356
    • Bennoun, P.1
  • 7
    • 0017277818 scopus 로고
    • Assay of proteins in the presence of interfering materials
    • Bensadoun A, Weinstein D (1976) Assay of proteins in the presence of interfering materials. Anal Biochem 70:241-250
    • (1976) Anal Biochem , vol.70 , pp. 241-250
    • Bensadoun, A.1    Weinstein, D.2
  • 8
    • 0002587507 scopus 로고
    • Studies on the expression of NDH-H, a subunit of the NAD(P)H-plastoquinone-oxidoreductase of higher-plant chloroplasts
    • Berger S, Ellersiek U, Westhoff P, Steinmüller K (1993) Studies on the expression of NDH-H, a subunit of the NAD(P)H-plastoquinone-oxidoreductase of higher-plant chloroplasts. Planta 190:25-31
    • (1993) Planta , vol.190 , pp. 25-31
    • Berger, S.1    Ellersiek, U.2    Westhoff, P.3    Steinmüller, K.4
  • 9
    • 0029142099 scopus 로고
    • Properties of a large complex with NADH dehydrogenase activity from barley thylakoids
    • Cuello J, Quiles MJ, Albacete ME, Sabater B (1995) Properties of a large complex with NADH dehydrogenase activity from barley thylakoids. Plant Cell Physiol 36:265-271
    • (1995) Plant Cell Physiol , vol.36 , pp. 265-271
    • Cuello, J.1    Quiles, M.J.2    Albacete, M.E.3    Sabater, B.4
  • 10
    • 0029059910 scopus 로고
    • The proton-pumping respiratory complex I of bacteria and mitochondria and its homologue of chloroplasts
    • Friedrich T, Steinmüller K, Weiss H (1995) The proton-pumping respiratory complex I of bacteria and mitochondria and its homologue of chloroplasts. FEBS Lett 367:107-111
    • (1995) FEBS Lett , vol.367 , pp. 107-111
    • Friedrich, T.1    Steinmüller, K.2    Weiss, H.3
  • 11
    • 14744291761 scopus 로고
    • Stable plastid transformation in PEG-treated protoplasts of Nicotiana tabacum
    • Golds TJ, Maliga P, Koop HU (1993) Stable plastid transformation in PEG-treated protoplasts of Nicotiana tabacum. Biotechnology 11:95-97
    • (1993) Biotechnology , vol.11 , pp. 95-97
    • Golds, T.J.1    Maliga, P.2    Koop, H.U.3
  • 12
    • 0030043480 scopus 로고    scopus 로고
    • Evidence for an association of ndhB, ndhJ gene products and ferredoxin-NADP-reductase as components of a chloroplastic NAD(P)H dehydrogenase complex
    • Guedeney G, Corneille S, Cuiné S, Peltier G (1996) Evidence for an association of ndhB, ndhJ gene products and ferredoxin-NADP-reductase as components of a chloroplastic NAD(P)H dehydrogenase complex. FEBS Lett 378:277-280
    • (1996) FEBS Lett , vol.378 , pp. 277-280
    • Guedeney, G.1    Corneille, S.2    Cuiné, S.3    Peltier, G.4
  • 13
    • 0027478870 scopus 로고
    • A transcription map of the chloroplast genome from rice (Oryza sativa)
    • Kanno A, Hirai A (1993) A transcription map of the chloroplast genome from rice (Oryza sativa). Curr Genet 23:166-174
    • (1993) Curr Genet , vol.23 , pp. 166-174
    • Kanno, A.1    Hirai, A.2
  • 14
    • 0021678736 scopus 로고
    • Electroblotting of multiple gels: A simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide gels to nitrocellulose
    • Khyse-Anderson J (1984) Electroblotting of multiple gels: a simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide gels to nitrocellulose. J Biochem Biophys Methods 10:203-209
    • (1984) J Biochem Biophys Methods , vol.10 , pp. 203-209
    • Khyse-Anderson, J.1
  • 15
    • 0002562002 scopus 로고
    • Plastid transformation by polyethylene glycol treatment of protoplasts and regeneration of trans-plastomic plants
    • Potrykus I, Spangenberg G (eds) Springer-Verlag, Berlin Heidelberg New York
    • Koop HU, Kofer W (1995) Plastid transformation by polyethylene glycol treatment of protoplasts and regeneration of trans-plastomic plants. In: Potrykus I, Spangenberg G (eds) Gene transfer in plants, Springer-Verlag, Berlin Heidelberg New York, pp 75-82
    • (1995) Gene Transfer in Plants , pp. 75-82
    • Koop, H.U.1    Kofer, W.2
  • 16
    • 0029818050 scopus 로고    scopus 로고
    • Integration of foreign sequences into the tobacco plastome via polyethylene glycol-mediated protoplast transformation
    • Koop HU, Steinmüller K, Wagner H, Rössler C, Eibl C, Sacher L (1996) Integration of foreign sequences into the tobacco plastome via polyethylene glycol-mediated protoplast transformation. Planta 199:193-201
    • (1996) Planta , vol.199 , pp. 193-201
    • Koop, H.U.1    Steinmüller, K.2    Wagner, H.3    Rössler, C.4    Eibl, C.5    Sacher, L.6
  • 17
  • 18
    • 0029740614 scopus 로고    scopus 로고
    • 4 plant Sorghum bicolor indicates that the complex I-homologous NAD(P)-plastoquinone oxidoreductase is involved in cyclic electron transport
    • 4 plant Sorghum bicolor indicates that the complex I-homologous NAD(P)-plastoquinone oxidoreductase is involved in cyclic electron transport. Planta 199:276-281
    • (1996) Planta , vol.199 , pp. 276-281
    • Kubicki, A.1    Funk, E.2    Westhoff, P.3    Steinmüller, K.4
  • 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 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0029075136 scopus 로고
    • Isolation and characterization of the proton-translocating NADH:ubiquinone oxidoreductase from Escherichia coli
    • Leif H, Sled VD, Ohnishi T, Weiss H, Friedrich T (1995) Isolation and characterization of the proton-translocating NADH:ubiquinone oxidoreductase from Escherichia coli. Eur J Biochem 230:538-548
    • (1995) Eur J Biochem , vol.230 , pp. 538-548
    • Leif, H.1    Sled, V.D.2    Ohnishi, T.3    Weiss, H.4    Friedrich, T.5
  • 21
    • 0027571755 scopus 로고
    • Towards plastid transformation in flowering plants
    • Maliga P (1993) Towards plastid transformation in flowering plants. Trends Biotech 11:101-106
    • (1993) Trends Biotech , vol.11 , pp. 101-106
    • Maliga, P.1
  • 22
    • 0029189537 scopus 로고
    • Photoactivation of the electron flow from NADPH to plastoquinone in spinach chloroplasts
    • Mano J, Miyake C, Schreiber U, Asada K (1995) Photoactivation of the electron flow from NADPH to plastoquinone in spinach chloroplasts. Plant Cell Physiol 36:1589-1598
    • (1995) Plant Cell Physiol , vol.36 , pp. 1589-1598
    • Mano, J.1    Miyake, C.2    Schreiber, U.3    Asada, K.4
  • 23
    • 0023476294 scopus 로고
    • Six chloroplast genes (ndhA-F) homologous to human mitochondrial genes encoding components of the respiratory chain NADH dehydrogenase are actively expressed: Determination of the splice sites in ndhA and ndhB pre-mRNAs
    • Matsubayashi T, Wakasugi T, Shinozaki K, Yamaguchi-Shinozaki K, Zaita N, Hidaka T, Meng BY, Ohto C, Tanaka M, Kato A, Maruyama T, Sugiura M (1987) Six chloroplast genes (ndhA-F) homologous to human mitochondrial genes encoding components of the respiratory chain NADH dehydrogenase are actively expressed: determination of the splice sites in ndhA and ndhB pre-mRNAs. Mol Gen Genet 210:385-393
    • (1987) Mol Gen Genet , vol.210 , pp. 385-393
    • Matsubayashi, T.1    Wakasugi, T.2    Shinozaki, K.3    Yamaguchi-Shinozaki, K.4    Zaita, N.5    Hidaka, T.6    Meng, B.Y.7    Ohto, C.8    Tanaka, M.9    Kato, A.10    Maruyama, T.11    Sugiura, M.12
  • 27
    • 0025896072 scopus 로고
    • Plasmid vectors for selecting IS1-promoted deletions in cloned DNA: Sequence analysis of the Omega interposon
    • Prentki P, Binda A, Epstein A (1991) Plasmid vectors for selecting IS1-promoted deletions in cloned DNA: sequence analysis of the Omega interposon. Gene 103: 17-23
    • (1991) Gene , vol.103 , pp. 17-23
    • Prentki, P.1    Binda, A.2    Epstein, A.3
  • 29
    • 0029792224 scopus 로고    scopus 로고
    • Detection and characterization of a complex I-like NADH-specific dehydrogenase from pea thylakoids
    • Sazanov LA, Burrows P, Nixon PJ (1996) Detection and characterization of a complex I-like NADH-specific dehydrogenase from pea thylakoids. Biochem Soc Trans 24:739-743
    • (1996) Biochem Soc Trans , vol.24 , pp. 739-743
    • Sazanov, L.A.1    Burrows, P.2    Nixon, P.J.3
  • 30
    • 0000347609 scopus 로고
    • Detection of rapid induction kinetics with a new type of high-frequency modulated chlorophyll fluorometer
    • Schreiber U (1986) Detection of rapid induction kinetics with a new type of high-frequency modulated chlorophyll fluorometer. Photosynth Res 9:261-272
    • (1986) Photosynth Res , vol.9 , pp. 261-272
    • Schreiber, U.1
  • 32
    • 0026860017 scopus 로고
    • The chloroplast genome
    • Sugiura M (1992) The chloroplast genome. Plant Mol Biol 19:149-168
    • (1992) Plant Mol Biol , vol.19 , pp. 149-168
    • Sugiura, M.1
  • 33
    • 0027398358 scopus 로고
    • High-frequency plastid transformation in tobacco by section for a chimeric aadA gene
    • Svab Z, Maliga P (1993) High-frequency plastid transformation in tobacco by section for a chimeric aadA gene. Proc Natl Acad Sci USA 90:913-917
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 913-917
    • Svab, Z.1    Maliga, P.2
  • 35
    • 34249958267 scopus 로고
    • The use of chlorophyll fluorescence nomenclature in plant stress physiology
    • Van Kooten O, Snel JFH (1990) The use of chlorophyll fluorescence nomenclature in plant stress physiology. Photosynth Res 25:147-150
    • (1990) Photosynth Res , vol.25 , pp. 147-150
    • Van Kooten, O.1    Snel, J.F.H.2
  • 36
    • 0027104114 scopus 로고
    • The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains
    • Walker JE (1992) The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains. Quart Rev Biophysics 25:253-324
    • (1992) Quart Rev Biophysics , vol.25 , pp. 253-324
    • Walker, J.E.1
  • 37
    • 0027519561 scopus 로고
    • The gene locus of the proton-translocating NADH:ubiquinone oxidoreductase in Escherichia coli
    • Weidner U, Geier S, Ptock A, Friedrich T, Leif H, Weiss H (1993) The gene locus of the proton-translocating NADH:ubiquinone oxidoreductase in Escherichia coli. J Mol Biol 233:109-122
    • (1993) J Mol Biol , vol.233 , pp. 109-122
    • Weidner, U.1    Geier, S.2    Ptock, A.3    Friedrich, T.4    Leif, H.5    Weiss, H.6
  • 38
    • 0025760073 scopus 로고
    • The respiratory-chain NADH dehydrogenase (complex I) of mitochondria
    • Weiss H, Friedrich T, Hofhaus G, Preis D (1991) The respiratory-chain NADH dehydrogenase (complex I) of mitochondria. Eur J Biochem 197:563-576
    • (1991) Eur J Biochem , vol.197 , pp. 563-576
    • Weiss, H.1    Friedrich, T.2    Hofhaus, G.3    Preis, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.