메뉴 건너뛰기




Volumn 124, Issue 1, 1997, Pages 33-40

Decrease in glycolate pathway enzyme activities in plastids and peroxisomes of the albostrians mutant of barley (Hordeum vulgare L.)

Author keywords

Glycolate pathway; Hordeum vulgare L.; Mutant (barley); Peroxisomes; Plastids; Ultrastructure

Indexed keywords

CATALASE; FUMARATE HYDRATASE; GLYCINE HYDROXYMETHYLTRANSFERASE; GLYCOLIC ACID; GLYOXYLIC ACID; HYDROXY ACID OXIDASE A; HYDROXYPYRUVATE REDUCTASE; ISOCITRATE LYASE; MALATE SYNTHASE; PHOSPHATASE; PLANT EXTRACT; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 0030910762     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-9452(97)04592-5     Document Type: Article
Times cited : (12)

References (43)
  • 1
    • 0001937302 scopus 로고
    • Ein fall gen-induzierter mutationen des plasmotyps bei gerste
    • R. Hagemann and F. Scholz, Ein Fall gen-induzierter Mutationen des Plasmotyps bei Gerste. Der Züchter, 32 (1962) 50-59.
    • (1962) Der Züchter , vol.32 , pp. 50-59
    • Hagemann, R.1    Scholz, F.2
  • 2
    • 0006840498 scopus 로고
    • Chloroplast control of nuclear gene function
    • T. Börner, Chloroplast control of nuclear gene function. Endocyt. Cell Res., 3 (1986) 265-274.
    • (1986) Endocyt. Cell Res. , vol.3 , pp. 265-274
    • Börner, T.1
  • 3
    • 21344488714 scopus 로고
    • Ribosomedeficient plastids of albostrians barley: Extreme representatives of non-photosynthetic plastids
    • W.R. Hess, T. Hübschmann and T. Börner. Ribosomedeficient plastids of albostrians barley: extreme representatives of non-photosynthetic plastids. Endocyt. Cell Res., 10 (1994) 65-80.
    • (1994) Endocyt. Cell Res. , vol.10 , pp. 65-80
    • Hess, W.R.1    Hübschmann, T.2    Börner, T.3
  • 4
    • 0028134068 scopus 로고
    • Aldolases in barley (Hordeum vulgare L.): Properties and repression of the plastid enzyme in the plastome mutant albostrians
    • R. Boldt, B. Pelzer-Reith, T. Börner and C. Schnarrenberger, Aldolases in barley (Hordeum vulgare L.): properties and repression of the plastid enzyme in the plastome mutant albostrians. J. Plant Physiol., 144 (1994) 282-286.
    • (1994) J. Plant Physiol. , vol.144 , pp. 282-286
    • Boldt, R.1    Pelzer-Reith, B.2    Börner, T.3    Schnarrenberger, C.4
  • 5
    • 0007860195 scopus 로고
    • Repression of the plastidic isoenzymes of aldolase, 3-phosphoglycerate kinase, and triosephosphate isomerase in the barley mutant albostrians
    • R. Boldt, T. Börner and C. Schnarrenberger, Repression of the plastidic isoenzymes of aldolase, 3-phosphoglycerate kinase, and triosephosphate isomerase in the barley mutant albostrians. Plant Physiol., 99 (1992) 895-900.
    • (1992) Plant Physiol. , vol.99 , pp. 895-900
    • Boldt, R.1    Börner, T.2    Schnarrenberger, C.3
  • 6
    • 0001385989 scopus 로고
    • Cytoplasmic synthesis of plastid polypeptides may be controlled by plastid-synthesized RNA
    • J.W. Bradbeer, Y.E. Atkinson, T. Börner and R. Hagemann, Cytoplasmic synthesis of plastid polypeptides may be controlled by plastid-synthesized RNA. Nature, 279 (1979) 816-817.
    • (1979) Nature , vol.279 , pp. 816-817
    • Bradbeer, J.W.1    Atkinson, Y.E.2    Börner, T.3    Hagemann, R.4
  • 7
    • 0028115708 scopus 로고
    • Ribosome-deflcient plastids affect transcription of light-induced nuclear genes: Genetic evidence for a plastid-derived signal
    • W.R. Hess, A. Müller, F. Nagy and T. Börner, Ribosome-deflcient plastids affect transcription of light-induced nuclear genes: genetic evidence for a plastid-derived signal. Mol. Gen. Genet., 242 (1994) 305-312.
    • (1994) Mol. Gen. Genet. , vol.242 , pp. 305-312
    • Hess, W.R.1    Müller, A.2    Nagy, F.3    Börner, T.4
  • 8
    • 0001630788 scopus 로고
    • Photo-oxidative destruction of chloroplasts and its consequences for expression of nuclear genes
    • R. Oelmüller and H. Mohr, Photo-oxidative destruction of chloroplasts and its consequences for expression of nuclear genes. Planta, 167 (1986) 106-113.
    • (1986) Planta , vol.167 , pp. 106-113
    • Oelmüller, R.1    Mohr, H.2
  • 9
    • 0001211235 scopus 로고
    • Regulatory interactions between nuclear and plastid genomes
    • W.C. Taylor, Regulatory interactions between nuclear and plastid genomes. Annu. Rev. Plant Physiol., 40 (1989) 211-233.
    • (1989) Annu. Rev. Plant Physiol. , vol.40 , pp. 211-233
    • Taylor, W.C.1
  • 10
    • 0342459480 scopus 로고
    • Regulation of nuclear gene expression for plastidogenesis as affected by the developmental stage of plastids
    • V.K. Rajasekhar, Regulation of nuclear gene expression for plastidogenesis as affected by the developmental stage of plastids. Biochem. Physiol. Pflanzen, 187 (1991) 257-271.
    • (1991) Biochem. Physiol. Pflanzen , vol.187 , pp. 257-271
    • Rajasekhar, V.K.1
  • 11
    • 0001196855 scopus 로고
    • A tale of two genomes: Role of a chloroplast signal in coordinating nuclear and plastid genome expression
    • R.E. Susek and J.C. Chory, A tale of two genomes: role of a chloroplast signal in coordinating nuclear and plastid genome expression. Aust. J. Plant Physiol., 19 (1992) 387-399.
    • (1992) Aust. J. Plant Physiol. , vol.19 , pp. 387-399
    • Susek, R.E.1    Chory, J.C.2
  • 12
    • 0000478533 scopus 로고
    • Microbodies - Peroxisomes and glyoxysomes
    • N.E. Tolbert, Microbodies - peroxisomes and glyoxysomes. Annu. Rev. Plant Physiol., 22 (1971) 45-74.
    • (1971) Annu. Rev. Plant Physiol. , vol.22 , pp. 45-74
    • Tolbert, N.E.1
  • 13
    • 0342893705 scopus 로고
    • Interactions among cell organelles involved in photorespiration
    • C.R. Stocking and U. Heber (Eds.), Springer, Heidelberg
    • C. Schnarrenberger and H. Fock, Interactions among cell organelles involved in photorespiration, in: C.R. Stocking and U. Heber (Eds.), Transport in Plants III, Encyclopedia of Plant Physiology (New Series), Vol 3, Springer, Heidelberg, 1976, pp. 185-234.
    • (1976) Transport in Plants III, Encyclopedia of Plant Physiology (New Series) , vol.3 , pp. 185-234
    • Schnarrenberger, C.1    Fock, H.2
  • 14
    • 0000170915 scopus 로고
    • Development of microbodies in sunflower cotyledons and castor bean endosperm during germination
    • C. Schnarrenberger, A. Oeser and N.E. Tolbert, Development of microbodies in sunflower cotyledons and castor bean endosperm during germination. Plant Physiol., 48 (1971) 466-474.
    • (1971) Plant Physiol. , vol.48 , pp. 466-474
    • Schnarrenberger, C.1    Oeser, A.2    Tolbert, N.E.3
  • 15
    • 0342459479 scopus 로고
    • Differential regulation of phosphoglycolate and phosphoglycerate phosphatase in Euglena
    • L. James and S.D. Schwartzbach, Differential regulation of phosphoglycolate and phosphoglycerate phosphatase in Euglena. Plant Sci. Lett., 27 (1982) 223-232.
    • (1982) Plant Sci. Lett. , vol.27 , pp. 223-232
    • James, L.1    Schwartzbach, S.D.2
  • 16
    • 3342922088 scopus 로고
    • A microcolorimetric method for determination of inorganic phosphorus
    • H.H. Taussky and E. Shorr, A microcolorimetric method for determination of inorganic phosphorus. J. Biol. Chem., 202 (1953) 675-685.
    • (1953) J. Biol. Chem. , vol.202 , pp. 675-685
    • Taussky, H.H.1    Shorr, E.2
  • 17
    • 0002823461 scopus 로고
    • Developmental studies on microbodies in wheat leaves. I: Conditions influencing enzyme development
    • J. Feierabend and H. Beevers, Developmental studies on microbodies in wheat leaves. I: conditions influencing enzyme development. Plant Physiol., 49 (1972) 28-32.
    • (1972) Plant Physiol. , vol.49 , pp. 28-32
    • Feierabend, J.1    Beevers, H.2
  • 18
    • 0002191974 scopus 로고
    • Catalase
    • H.U. Bergmeyer (Ed.), Academic Press, New York
    • H. Lück, Catalase, in: H.U. Bergmeyer (Ed.), Methods in Enzymatic Analysis, Academic Press, New York, 1965, pp. 885-894.
    • (1965) Methods in Enzymatic Analysis , pp. 885-894
    • Lück, H.1
  • 19
    • 0343328760 scopus 로고
    • Properties and intramitochondrial localization of serine hydroxymethyltransferals transferase in leaves of higher plants
    • K.C. Woo, Properties and intramitochondrial localization of serine hydroxymethyltransferals transferase in leaves of higher plants. Plant Physiol., 63 (1979) 783-787.
    • (1979) Plant Physiol. , vol.63 , pp. 783-787
    • Woo, K.C.1
  • 20
    • 0023296158 scopus 로고
    • NADH: Hydroxypyruvate reductase and NADPH: Glyoxylate reductase in algae. Partial purification and characterization from Chlamydomonas reinhardtii
    • D.W. Husic and N.E. Tolbert, NADH: hydroxypyruvate reductase and NADPH: glyoxylate reductase in algae: partial purification and characterization from Chlamydomonas reinhardtii. Arch Biochem. Biophys., 252 (1987) 396-408.
    • (1987) Arch Biochem. Biophys. , vol.252 , pp. 396-408
    • Husic, D.W.1    Tolbert, N.E.2
  • 22
    • 0014940410 scopus 로고
    • Localization and properties of hydroxypyruvate and glyoxylate reductases in spinach leaf particles
    • N.E. Tolbert, R.K. Yamazaki and A. Oeser, Localization and properties of hydroxypyruvate and glyoxylate reductases in spinach leaf particles. J Biol. Chem., 245 (1970) 5129-5136.
    • (1970) J Biol. Chem. , vol.245 , pp. 5129-5136
    • Tolbert, N.E.1    Yamazaki, R.K.2    Oeser, A.3
  • 23
    • 0001904522 scopus 로고
    • Assay methods for key enzymes of the glycolate cycle
    • G.H. Dixon and H.L. Kornberg, Assay methods for key enzymes of the glycolate cycle. Biochem. J., 72 (1959) 3.
    • (1959) Biochem. J. , vol.72 , pp. 3
    • Dixon, G.H.1    Kornberg, H.L.2
  • 24
    • 77956989479 scopus 로고
    • Malate synthetase from bakers yeast
    • G.H. Dixon and H.L. Kornberg, Malate synthetase from bakers yeast. Methods Enzymol., 5 (1962) 633-637.
    • (1962) Methods Enzymol. , vol.5 , pp. 633-637
    • Dixon, G.H.1    Kornberg, H.L.2
  • 25
    • 0014670328 scopus 로고
    • Mitochondria and glyoxisomes from castor bean endosperm: Enzyme constituents and catalytic capacity
    • T. Cooper and H. Beevers, Mitochondria and glyoxisomes from castor bean endosperm: enzyme constituents and catalytic capacity. J. Biol. Chem., 244 (1969) 3507-3513.
    • (1969) J. Biol. Chem. , vol.244 , pp. 3507-3513
    • Cooper, T.1    Beevers, H.2
  • 26
    • 0001512589 scopus 로고
    • + messenger RNA from higher plants
    • M. Edelmann, R.B. Hallick and H.H. Chua (Eds.), Elsevier Biomedical Press, Amsterdam
    • + messenger RNA from higher plants, in: M. Edelmann, R.B. Hallick and H.H. Chua (Eds.), Methods in Chloroplast Molecular Biology, Elsevier Biomedical Press, Amsterdam, 1982, pp. 387-393.
    • (1982) Methods in Chloroplast Molecular Biology , pp. 387-393
    • Cashmore, A.R.1
  • 27
    • 0017643426 scopus 로고
    • RNA molecular weight detemination by gel electrophoresis under denaturing conditions
    • H. Lehrach, D. Diomond, J.M. Wozney and H. Boedtker. RNA molecular weight detemination by gel electrophoresis under denaturing conditions. Biochemistry, 16 (1977) 4743-4751.
    • (1977) Biochemistry , vol.16 , pp. 4743-4751
    • Lehrach, H.1    Diomond, D.2    Wozney, J.M.3    Boedtker, H.4
  • 29
    • 0020793569 scopus 로고
    • A technique for radiolabeling restriction endonuclease fragments to high specific activity
    • A.P. Feinberg and B. Vogelstein, A technique for radiolabeling restriction endonuclease fragments to high specific activity. Anal. Biochem., 132 (1983) 6-13.
    • (1983) Anal. Biochem. , vol.132 , pp. 6-13
    • Feinberg, A.P.1    Vogelstein, B.2
  • 30
    • 0023434086 scopus 로고
    • Isolation and characterization of a cDNA clone for the Cat2 gene in maize and its homology with other catalases
    • L.A. Bethards, R.W. Skadsen and J.G. Scandalios, Isolation and characterization of a cDNA clone for the Cat2 gene in maize and its homology with other catalases. Proc. Natl. Acad. Sci. USA, 84 (1987) 6830-6834.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6830-6834
    • Bethards, L.A.1    Skadsen, R.W.2    Scandalios, J.G.3
  • 31
    • 0023665350 scopus 로고
    • The primary structure of spinach glycolate oxidase deduced from the DNA sequence of a cDNA clone
    • M. Volokita and C.R. Somerville, The primary structure of spinach glycolate oxidase deduced from the DNA sequence of a cDNA clone. J. Biol. Chem. 262 (1987) 15825-15828.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15825-15828
    • Volokita, M.1    Somerville, C.R.2
  • 32
    • 0014608724 scopus 로고
    • Cytochemical localization of catalase in leaf microbodies (peroxisomes)
    • S.E. Frederick and E.H. Newcomb, Cytochemical localization of catalase in leaf microbodies (peroxisomes). J. Cell Biol., 43 (1969) 343-353.
    • (1969) J. Cell Biol. , vol.43 , pp. 343-353
    • Frederick, S.E.1    Newcomb, E.H.2
  • 33
    • 0014444144 scopus 로고
    • A low viscosity epoxy resin embedding medium for electron microscopy
    • A.R. Spurr, A low viscosity epoxy resin embedding medium for electron microscopy. J. Ultrastruct. Res., 26 (1969) 31-43.
    • (1969) J. Ultrastruct. Res. , vol.26 , pp. 31-43
    • Spurr, A.R.1
  • 34
    • 0000964508 scopus 로고
    • Glyoxysome microbodies in senescent spinach leaves
    • R. Landolt and P. Matile, Glyoxysome microbodies in senescent spinach leaves. Plant Sci., 72 (1990) 159-163.
    • (1990) Plant Sci. , vol.72 , pp. 159-163
    • Landolt, R.1    Matile, P.2
  • 35
    • 0029200019 scopus 로고
    • Evidence for three serine hydroxymethyltransferases in green leaf cells: Purification and characterization of the mitochondrial and chloroplastic isoforms
    • V. Besson, M. Neuburger, F. Rebeille and R. Douce, Evidence for three serine hydroxymethyltransferases in green leaf cells: purification and characterization of the mitochondrial and chloroplastic isoforms. Plant Physiol. and Biochem., 33 (1995) 665-673.
    • (1995) Plant Physiol. and Biochem. , vol.33 , pp. 665-673
    • Besson, V.1    Neuburger, M.2    Rebeille, F.3    Douce, R.4
  • 36
    • 0029869004 scopus 로고    scopus 로고
    • Mitochondria are a major site for folate and thymidylate synthesis in plants
    • M. Neuburger, F. Rebeille, A. Jourdain. S. Nakamura and R. Douce, Mitochondria are a major site for folate and thymidylate synthesis in plants. J. Biol. Chem., 271 (1996) 9466-9472.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9466-9472
    • Neuburger, M.1    Rebeille, F.2    Jourdain, A.3    Nakamura, S.4    Douce, R.5
  • 37
    • 0000800864 scopus 로고
    • Enzymes of serine and glycine metabolism in leaves and non-photosynthetic tissue of Pisum sativum L
    • N.J. Walton and H.W. Woolhouse, Enzymes of serine and glycine metabolism in leaves and non-photosynthetic tissue of Pisum sativum L. Planta, 167 (1986) 114-128.
    • (1986) Planta , vol.167 , pp. 114-128
    • Walton, N.J.1    Woolhouse, H.W.2
  • 38
    • 0001543316 scopus 로고
    • Light dependence of catalase synthesis and degradation in leaves and influence of interfering stress conditions
    • B. Hertwig, P. Streb and J. Feierabend, Light dependence of catalase synthesis and degradation in leaves and influence of interfering stress conditions. Plant Physiol., 100 (1992) 1547-1553.
    • (1992) Plant Physiol. , vol.100 , pp. 1547-1553
    • Hertwig, B.1    Streb, P.2    Feierabend, J.3
  • 39
    • 0000405836 scopus 로고
    • Photoinactivation of catalase occurs under both high-and low-temperature stress conditions and accompanies photo-inhibition of photosystem II
    • J. Feierabend, C. Schaan and B. Hertwig, Photoinactivation of catalase occurs under both high-and low-temperature stress conditions and accompanies photo-inhibition of photosystem II. Plant Physiol., 100 (1992) 1554-1561.
    • (1992) Plant Physiol. , vol.100 , pp. 1554-1561
    • Feierabend, J.1    Schaan, C.2    Hertwig, B.3
  • 40
    • 0242532145 scopus 로고
    • Chlorophyll and carotenoid content of ribosome-deficient plastids
    • T. Börner and A. Meister, Chlorophyll and carotenoid content of ribosome-deficient plastids. Photosynthetica, 14 (1980) 589-593.
    • (1980) Photosynthetica , vol.14 , pp. 589-593
    • Börner, T.1    Meister, A.2
  • 41
    • 0000266933 scopus 로고
    • Nitrate reductase is not accumulated in chloroplast-ribosome deficient mutants of higher plants
    • T. Börner, R.R. Mendel and J. Schiemann, Nitrate reductase is not accumulated in chloroplast-ribosome deficient mutants of higher plants. Planta, 169 (1986) 202-207.
    • (1986) Planta , vol.169 , pp. 202-207
    • Börner, T.1    Mendel, R.R.2    Schiemann, J.3
  • 42
    • 0002999107 scopus 로고
    • Coordinated expression of photosynthetic and photorespiratory genes
    • A Brennicke and U. Kück (Eds.), Verlag Chemie. Weinheim
    • R. Srinivasan, W.A. Berndt and D.J. Oliver, Coordinated expression of photosynthetic and photorespiratory genes, in: A Brennicke and U. Kück (Eds.), Plant Mitochondria, Verlag Chemie. Weinheim, 1993, pp. 241-250.
    • (1993) Plant Mitochondria , pp. 241-250
    • Srinivasan, R.1    Berndt, W.A.2    Oliver, D.J.3
  • 43
    • 0001965083 scopus 로고
    • Altered nuclear, mitochondrial and plastid gene expression in white barley cells containing ribosome-deficient plastids
    • A. Brennicke and U. Kück (Eds.). Verlag Chemie, Weinheim
    • T. Börner and W.R. Hess, Altered nuclear, mitochondrial and plastid gene expression in white barley cells containing ribosome-deficient plastids. in: A. Brennicke and U. Kück (Eds.), Plant Mitochondria. Verlag Chemie, Weinheim, 1993. pp. 207-219.
    • (1993) Plant Mitochondria , pp. 207-219
    • Börner, T.1    Hess, W.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.