메뉴 건너뛰기




Volumn 104, Issue 1, 1998, Pages 116-124

A spontaneous point mutation in the Rubisco large subunit gene impairing holoenzyme assembly renders the IVβ plastome mutant of Oenothera extremely light- and chilling sensitive

Author keywords

Chlorophyll fluorescence; Oenothera; Plastome mutant; Rubisco

Indexed keywords

AMINO ACID ANALYSIS; CARBON DIOXIDE FIXATION; CHAPERONINE 60; CHLOROPHYLL; CHLOROPLAST GENETICS; FLUORESCENCE; GENOTYPE; HOLOENZYME; MUTANT; OXYGEN; POINT MUTATION; VIOLAXANTHIN;

EID: 0031787172     PISSN: 00319317     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3054.1998.1040115.x     Document Type: Article
Times cited : (5)

References (42)
  • 1
    • 0024432773 scopus 로고
    • A point mutation in the gene tor the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase affects holoenzyme assembly in Nicotiana tabacum
    • Avni, A., Edelman, M., Rachailovich, I., Avni, D. & Fluhr, R. 1989. A point mutation in the gene tor the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase affects holoenzyme assembly in Nicotiana tabacum. - EMBO J. 8: 1915-1918.
    • (1989) EMBO J. , vol.8 , pp. 1915-1918
    • Avni, A.1    Edelman, M.2    Rachailovich, I.3    Avni, D.4    Fluhr, R.5
  • 2
    • 0000191368 scopus 로고
    • Photosynthetic response and adaptation to temperature in higher plants
    • Berry, J. O. & Björkman, O. 1980. Photosynthetic response and adaptation to temperature in higher plants. - Annu. Rev. Plant Physiol. 31: 491-543.
    • (1980) Annu. Rev. Plant Physiol. , vol.31 , pp. 491-543
    • Berry, J.O.1    Björkman, O.2
  • 3
    • 0001581061 scopus 로고
    • Temperature dependence of violaxanthin deepoxidation and non-photochemical fluorescence quenching in intact leaves of Gossypium hirsutum L. and Malva parviflora L.
    • Bilger, W. & Björkman, O. 1991. Temperature dependence of violaxanthin deepoxidation and non-photochemical fluorescence quenching in intact leaves of Gossypium hirsutum L. and Malva parviflora L. - Planta 184: 226-234.
    • (1991) Planta , vol.184 , pp. 226-234
    • Bilger, W.1    Björkman, O.2
  • 4
    • 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. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. - Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0000929912 scopus 로고
    • Low-temperature limitations of photosynthesis in three tropical Vigna species: A chlorophyll fluorescence study
    • Brüggemann, W. 1992. Low-temperature limitations of photosynthesis in three tropical Vigna species: A chlorophyll fluorescence study. - Photosynth. Res. 34: 301-310.
    • (1992) Photosynth. Res. , vol.34 , pp. 301-310
    • Brüggemann, W.1
  • 6
    • 0000440908 scopus 로고
    • Chilling sensitivity of photosynthesis: Ecophysiological studies in two Lycopersicon species of different chilling tolerance
    • - , Dauborn, B., Klaucke, S., Linger, P., Maas-Kantel, K. & Wenner, A. 1995. Chilling sensitivity of photosynthesis: Ecophysiological studies in two Lycopersicon species of different chilling tolerance. - Acta Physiol. Plant. 17: 113-122.
    • (1995) Acta Physiol. Plant. , vol.17 , pp. 113-122
    • Dauborn, B.1    Klaucke, S.2    Linger, P.3    Maas-Kantel, K.4    Wenner, A.5
  • 9
    • 0002832747 scopus 로고    scopus 로고
    • Genome and plastome effects on photosynthesis parameters in Oenothera species of differential low-temperature tolerance
    • Dauborn, B. & Brüggemann, W. 1996. Genome and plastome effects on photosynthesis parameters in Oenothera species of differential low-temperature tolerance. - Physiol. Plant. 97: 79-84.
    • (1996) Physiol. Plant. , vol.97 , pp. 79-84
    • Dauborn, B.1    Brüggemann, W.2
  • 10
    • 0001938338 scopus 로고    scopus 로고
    • The role of xanthophyll cycle carotenoids in the protection of photosynthesis
    • Demmig-Adams, B. & Adams, W. W. 1996. The role of xanthophyll cycle carotenoids in the protection of photosynthesis. - Trends Plant Sci. 1: 21-26.
    • (1996) Trends Plant Sci. , vol.1 , pp. 21-26
    • Demmig-Adams, B.1    Adams, W.W.2
  • 11
    • 0001147694 scopus 로고
    • Genome composition of asymmetric hybrids in relation to the phylogenetic distance between the parents. Nucleus-chloroplast interactions
    • Derks, F. H. M., Hakkert, J. C., Verbeek, J. C. & Colijn-Hooymans, C. M. 1992. Genome composition of asymmetric hybrids in relation to the phylogenetic distance between the parents. Nucleus-chloroplast interactions. - Theor. Appl. Genet. 84: 930-940.
    • (1992) Theor. Appl. Genet. , vol.84 , pp. 930-940
    • Derks, F.H.M.1    Hakkert, J.C.2    Verbeek, J.C.3    Colijn-Hooymans, C.M.4
  • 12
    • 0031401064 scopus 로고    scopus 로고
    • Dynamics of xanthophyll-cycle activity in different antenna subcomplexes in the photosynthetic membranes of higher plants
    • Färber, A., Young, A. J., Ruban, A. V., Horton, P. & Jahns, P. 1997. Dynamics of xanthophyll-cycle activity in different antenna subcomplexes in the photosynthetic membranes of higher plants. - Plant Physiol. 115: 1609-1618.
    • (1997) Plant Physiol. , vol.115 , pp. 1609-1618
    • Färber, A.1    Young, A.J.2    Ruban, A.V.3    Horton, P.4    Jahns, P.5
  • 13
    • 2642712518 scopus 로고    scopus 로고
    • Effects of abiotic stress on the turnover of the D1 reaction centre II protein
    • Giardi, M. T., Masodijek, J. & Godde, D. 1997. Effects of abiotic stress on the turnover of the D1 reaction centre II protein. - Physiol. Plant. 101: 635-642.
    • (1997) Physiol. Plant. , vol.101 , pp. 635-642
    • Giardi, M.T.1    Masodijek, J.2    Godde, D.3
  • 15
    • 0028245595 scopus 로고
    • Structure, function, regulation and assembly of ribulose-1,5-bisphosphate carboxylase/oxygenase
    • Hartmann, F. C. & Harpel, M. R. 1994. Structure, function, regulation and assembly of ribulose-1,5-bisphosphate carboxylase/oxygenase. - Annu. Rev. Biochem. 63: 197-234.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 197-234
    • Hartmann, F.C.1    Harpel, M.R.2
  • 16
    • 0001419896 scopus 로고
    • Changes in the activities of enzymes of carbon metabolism in leaves during exposure of plants to low temperature
    • Holaday, A. S., Martindale, W., Alred, R., Brooks, A. L. & Leegood, R. C. 1992. Changes in the activities of enzymes of carbon metabolism in leaves during exposure of plants to low temperature. Plant Physiol. 98: 1105-1114.
    • (1992) Plant Physiol. , vol.98 , pp. 1105-1114
    • Holaday, A.S.1    Martindale, W.2    Alred, R.3    Brooks, A.L.4    Leegood, R.C.5
  • 17
    • 0000467650 scopus 로고
    • Reduction of ribulose-1,5-bisphosphate carboxylase/oxygenase content by antisense RNA reduces photosynthesis in tobacco plants
    • Hudson, G. S., Evans, J. R., von Caemmerer, S., Arvidsson, Y. B. & Andrews, T. J. 1992. Reduction of ribulose-1,5-bisphosphate carboxylase/oxygenase content by antisense RNA reduces photosynthesis in tobacco plants. - Plant Physiol. 98: 294-302.
    • (1992) Plant Physiol. , vol.98 , pp. 294-302
    • Hudson, G.S.1    Evans, J.R.2    Von Caemmerer, S.3    Arvidsson, Y.B.4    Andrews, T.J.5
  • 18
    • 0027995068 scopus 로고
    • Xanthophyll cycle and energy-dependent fluorescence quenching in leaves from pea plants grown under intermittent light
    • Jahns, P. & Krause, G. H. 1994. Xanthophyll cycle and energy-dependent fluorescence quenching in leaves from pea plants grown under intermittent light. - Planta 192: 176-182.
    • (1994) Planta , vol.192 , pp. 176-182
    • Jahns, P.1    Krause, G.H.2
  • 19
    • 0022484665 scopus 로고
    • UV crosslinking of RNA to nylon membranes enhances hybridization signals
    • Khandjian, E. W. 1986. UV crosslinking of RNA to nylon membranes enhances hybridization signals. - Mol. Biol. Rep. 11: 107-115.
    • (1986) Mol. Biol. Rep. , vol.11 , pp. 107-115
    • Khandjian, E.W.1
  • 20
    • 0025160560 scopus 로고
    • Crystallographic analysis of ribulose-1,5-bisphosphate carboxylase from spinach at 2.4 Å resolution. Subunit interaction and active site
    • Knight, S., Andersson, I. & Bränden, C. I. 1990. Crystallographic analysis of ribulose-1,5-bisphosphate carboxylase from spinach at 2.4 Å resolution. Subunit interaction and active site. - J. Mol. Biol. 215: 113-160.
    • (1990) J. Mol. Biol. , vol.215 , pp. 113-160
    • Knight, S.1    Andersson, I.2    Bränden, C.I.3
  • 21
    • 0028191820 scopus 로고
    • Photoinhibition, xanthophyll cycle and in vivo chlorophyll fluorescence quenching of chilling-tolerant Oxyria digyna and chilling-sensitive Zea mays
    • Koroleva, O. Y., Brüggemann, W. & Krause, G. H. 1994. Photoinhibition, xanthophyll cycle and in vivo chlorophyll fluorescence quenching of chilling-tolerant Oxyria digyna and chilling-sensitive Zea mays. - Physiol. Plant. 92: 577-584.
    • (1994) Physiol. Plant. , vol.92 , pp. 577-584
    • Koroleva, O.Y.1    Brüggemann, W.2    Krause, G.H.3
  • 23
    • 0001874273 scopus 로고
    • Investigations on plastome mutants in Oenothera. I. General considerations
    • Kutzelnigg, H. & Stubbe, W. 1974. Investigations on plastome mutants in Oenothera. I. General considerations. - Sub-Cell Biochem. 3: 73-89.
    • (1974) Sub-Cell Biochem. , vol.3 , pp. 73-89
    • Kutzelnigg, H.1    Stubbe, W.2
  • 24
    • 0021678736 scopus 로고
    • Electroblotting of multiple gels: A simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose
    • Kyhse-Anderson, J. 1984. Electroblotting of multiple gels: A simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose. - J. Biochem. Biophys. Methods 10: 203-209.
    • (1984) J. Biochem. Biophys. Methods , vol.10 , pp. 203-209
    • Kyhse-Anderson, J.1
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 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
  • 26
    • 0016168192 scopus 로고
    • An improved spectrophotometric assay for ribulose bisphosphate carboxylase
    • Lilley, R. M. C. & Walker, D. A. 1974. An improved spectrophotometric assay for ribulose bisphosphate carboxylase. - Biochim. Biophys. Acta 358: 226-229.
    • (1974) Biochim. Biophys. Acta , vol.358 , pp. 226-229
    • Lilley, R.M.C.1    Walker, D.A.2
  • 27
    • 0000890081 scopus 로고
    • Analysis of single and double-stranded nucleic acids on polyacrylamide and agarose gels by using glyoxal and acridin orange
    • McMaster, G. K. & Carmichael, G. G. 1977. Analysis of single and double-stranded nucleic acids on polyacrylamide and agarose gels by using glyoxal and acridin orange. -Proc. Natl. Acad. Sci. USA 74: 4835-4838.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 4835-4838
    • McMaster, G.K.1    Carmichael, G.G.2
  • 28
    • 0019321718 scopus 로고
    • Rapid isolation of high molecular weight plant DNA
    • Murray, M. G. & Thompson, W. F. 1980. Rapid isolation of high molecular weight plant DNA. - Nucleic Acids Res. 19: 4321-4325.
    • (1980) Nucleic Acids Res. , vol.19 , pp. 4321-4325
    • Murray, M.G.1    Thompson, W.F.2
  • 29
    • 0021328927 scopus 로고
    • Nucleotide sequence of the ribulose bisphosphate carboxylase gene from Rhodospirillum rubrum
    • Nargang, F., McIntosh, L. & Sommerville, C. 1984. Nucleotide sequence of the ribulose bisphosphate carboxylase gene from Rhodospirillum rubrum. - Mol. Gen. Genet. 193: 220-224.
    • (1984) Mol. Gen. Genet. , vol.193 , pp. 220-224
    • Nargang, F.1    McIntosh, L.2    Sommerville, C.3
  • 30
    • 0013925697 scopus 로고
    • Spinach ribulose diphosphate carboxylase. I. Purification and properties of the enzyme
    • Paulsen, J. M. & Lane, M. D. 1966. Spinach ribulose diphosphate carboxylase. I. Purification and properties of the enzyme. - Biochemistry 5: 2350-2357.
    • (1966) Biochemistry , vol.5 , pp. 2350-2357
    • Paulsen, J.M.1    Lane, M.D.2
  • 31
    • 0028310069 scopus 로고
    • Regulation and possible function of the xanthophyll cycle
    • Pfündel, E. & Bilger, W. 1994. Regulation and possible function of the xanthophyll cycle. - Photosynth. Res. 42: 89-109.
    • (1994) Photosynth. Res. , vol.42 , pp. 89-109
    • Pfündel, E.1    Bilger, W.2
  • 32
    • 0024314106 scopus 로고
    • An examination of factors contributing to non-photochemical quenching of chlorophyll fluorescence in barley leaves
    • Quick, W. P. & Stitt, M. 1989. An examination of factors contributing to non-photochemical quenching of chlorophyll fluorescence in barley leaves. - Biochim. Biophys. Acta 977: 287-296.
    • (1989) Biochim. Biophys. Acta , vol.977 , pp. 287-296
    • Quick, W.P.1    Stitt, M.2
  • 34
    • 0000153336 scopus 로고
    • Untersuchungen an strahleninduzierten Blattfarbenmutanten von Arabidopsis thaliana (L.) Heynh
    • Roebbelen, G. 1957. Untersuchungen an strahleninduzierten Blattfarbenmutanten von Arabidopsis thaliana (L.) Heynh. - Z. Indukt. Abstamm. Vererbungsl. 88: 189-252.
    • (1957) Z. Indukt. Abstamm. Vererbungsl. , vol.88 , pp. 189-252
    • Roebbelen, G.1
  • 37
    • 34250126784 scopus 로고
    • Continuous recording of photochemical and non-photochemical chlorophyll fluorescence quenching with a new type of modulation fluorometer
    • Schreiber, U., Schliwa, W. & Bilger, W. 1986. Continuous recording of photochemical and non-photochemical chlorophyll fluorescence quenching with a new type of modulation fluorometer. - Photosynth. Res. 10: 51-62.
    • (1986) Photosynth. Res. , vol.10 , pp. 51-62
    • Schreiber, U.1    Schliwa, W.2    Bilger, W.3
  • 38
    • 84994971792 scopus 로고
    • Does Rubisco control the rate of photosynthesis and plant growth? An exercise in molecular ecophysiology
    • Stitt, M. & Schulze, D. 1994. Does Rubisco control the rate of photosynthesis and plant growth? An exercise in molecular ecophysiology. - Plant Cell Environ. 17: 465-487.
    • (1994) Plant Cell Environ. , vol.17 , pp. 465-487
    • Stitt, M.1    Schulze, D.2
  • 39
    • 0026773744 scopus 로고
    • Conformational states of ribulosebisphosphate carboxylase and their interaction with chaperonin 60
    • van der Vies, S. M., Viitanen, P. V., Gatenby, A. A., Lorimer, G. H. & Jaenicke, R. 1992. Conformational states of ribulosebisphosphate carboxylase and their interaction with chaperonin 60. - Biochemistry 31: 3635-3644.
    • (1992) Biochemistry , vol.31 , pp. 3635-3644
    • Van Der Vies, S.M.1    Viitanen, P.V.2    Gatenby, A.A.3    Lorimer, G.H.4    Jaenicke, R.5
  • 40
    • 0000691858 scopus 로고
    • Differential accumulation of plastid transcripts encoding photosystem II components in the mesophyll and bundle-sheat cells of monocotyledonous NADP-malic enzyme-type C4 plants
    • Westhoff, P., Offermann-Steinhard, K., Höfer, M., Eskins, K., Oswald, A. & Streubel, M. 1991. Differential accumulation of plastid transcripts encoding photosystem II components in the mesophyll and bundle-sheat cells of monocotyledonous NADP-malic enzyme-type C4 plants. - Planta 184: 377-388.
    • (1991) Planta , vol.184 , pp. 377-388
    • Westhoff, P.1    Offermann-Steinhard, K.2    Höfer, M.3    Eskins, K.4    Oswald, A.5    Streubel, M.6
  • 41
    • 0041335118 scopus 로고
    • A five-base-pair-deletion in the gene for the large subunit causes the lesion in the ribulose bisphosphate carboxylase/oxygenase-deficient plastome mutant sigma of Oenothera hookeri
    • Winter, P. & Herrmann, R. G. 1988. A five-base-pair-deletion in the gene for the large subunit causes the lesion in the ribulose bisphosphate carboxylase/oxygenase-deficient plastome mutant sigma of Oenothera hookeri. - Bot. Acta 101: 1-56.
    • (1988) Bot. Acta , vol.101 , pp. 1-56
    • Winter, P.1    Herrmann, R.G.2
  • 42
    • 77957000603 scopus 로고
    • Ribulose diphosphate carboxylase from spinach leaves
    • Wishnick, M. & Lane, M. D. 1971. Ribulose diphosphate carboxylase from spinach leaves. - Methods Enzymol. 23: 570-577.
    • (1971) Methods Enzymol. , vol.23 , pp. 570-577
    • Wishnick, M.1    Lane, M.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.