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Volumn 11, Issue 3, 1999, Pages 335-347

The Arabidopsis photomorphogenic mutant HY1 is deficient in phytochrome chromophore biosynthesis as a result of a mutation in a plastid heme oxygenase

Author keywords

[No Author keywords available]

Indexed keywords

CHROMATOPHORE; ENZYME ACTIVITY; HEME OXYGENASE; MUTATION; PHYTOCHROME; PLASTID;

EID: 0033101492     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.11.3.335     Document Type: Article
Times cited : (280)

References (67)
  • 2
    • 0001812586 scopus 로고
    • Light-regulated expression of the nitrate reductase and nitrite reductase genes in tomato and in the phytochrome-deficient aurea mutant of tomato
    • Becker, T.W., Foyer, C., and Caboche, M. (1992). Light-regulated expression of the nitrate reductase and nitrite reductase genes in tomato and in the phytochrome-deficient aurea mutant of tomato. Planta 188, 39-47.
    • (1992) Planta , vol.188 , pp. 39-47
    • Becker, T.W.1    Foyer, C.2    Caboche, M.3
  • 3
    • 0021771482 scopus 로고
    • Binary Agrobacterium vectors for plant transformation
    • Bevan, M. (1984). Binary Agrobacterium vectors for plant transformation. Nucleic Acids Res. 12, 8711-8721.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 8711-8721
    • Bevan, M.1
  • 4
    • 0028534876 scopus 로고
    • Emerging themes of plant signal transduction
    • Bowler, C., and Chua, N.-H. (1994). Emerging themes of plant signal transduction. Plant Cell 6, 1529-1541.
    • (1994) Plant Cell , vol.6 , pp. 1529-1541
    • Bowler, C.1    Chua, N.-H.2
  • 8
    • 0000756654 scopus 로고
    • Different roles for phytochrome in etiolated and green plants deduced from characterization of Arabidopsis thaliana mutants
    • Chory, J., Peto, C.A., Ashbaugh, M., Saganich, R., Pratt, L., and Ausubel, F. (1989). Different roles for phytochrome in etiolated and green plants deduced from characterization of Arabidopsis thaliana mutants. Plant Cell 1, 867-880.
    • (1989) Plant Cell , vol.1 , pp. 867-880
    • Chory, J.1    Peto, C.A.2    Ashbaugh, M.3    Saganich, R.4    Pratt, L.5    Ausubel, F.6
  • 11
    • 0028450080 scopus 로고
    • The phytochrome apoprotein family in Arabidopsis is encoded by five genes: The sequences and expression of PHYD and PHYE
    • Clack, T., Mathews, S., and Sharrock, R.A. (1994). The phytochrome apoprotein family in Arabidopsis is encoded by five genes: The sequences and expression of PHYD and PHYE. Plant Mol. Biol. 25, 413-427.
    • (1994) Plant Mol. Biol. , vol.25 , pp. 413-427
    • Clack, T.1    Mathews, S.2    Sharrock, R.A.3
  • 12
    • 0022431959 scopus 로고
    • Precursors to two nuclear-encoded chloroplast proteins bind to the outer envelope membrane before being imported into chloroplasts
    • Cline, K., Werner-Washburne, M., Lubben, T.H., and Keegstra, K. (1985). Precursors to two nuclear-encoded chloroplast proteins bind to the outer envelope membrane before being imported into chloroplasts. J. Biol. Chem. 260, 3691-3696.
    • (1985) J. Biol. Chem. , vol.260 , pp. 3691-3696
    • Cline, K.1    Werner-Washburne, M.2    Lubben, T.H.3    Keegstra, K.4
  • 13
    • 0024297082 scopus 로고
    • Algal heme oxygenase from Cyanidium caldarium
    • Cornejo, J., and Beale, S.I. (1988). Algal heme oxygenase from Cyanidium caldarium. J. Biol. Chem. 263, 11915-11921.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11915-11921
    • Cornejo, J.1    Beale, S.I.2
  • 14
    • 0026729104 scopus 로고
    • Phytochrome assembly, the structure and biological activity of 2(R),3(E)-phytochromobilin derived from phycobiliproteins
    • Cornejo, J., Beale, S.I., Terry, M.J., and Lagarias, J.C. (1992). Phytochrome assembly, the structure and biological activity of 2(R),3(E)-phytochromobilin derived from phycobiliproteins. J. Biol. Chem. 267, 14790-14798.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14790-14798
    • Cornejo, J.1    Beale, S.I.2    Terry, M.J.3    Lagarias, J.C.4
  • 15
    • 0024962346 scopus 로고
    • Formation of a photoreversible phycocyanobilin-apophytochrome adduct in vitro
    • Elich, T.D., and Lagarias, J.C. (1989). Formation of a photoreversible phycocyanobilin-apophytochrome adduct in vitro. J. Biol. Chem. 264, 12902-12908.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12902-12908
    • Elich, T.D.1    Lagarias, J.C.2
  • 16
    • 0025135468 scopus 로고
    • A conserved cleavage-site motif in chloroplast transit peptides
    • Gavel, Y., and von Heijne, G. (1990). A conserved cleavage-site motif in chloroplast transit peptides. FEBS Lett. 261, 455-458.
    • (1990) FEBS Lett. , vol.261 , pp. 455-458
    • Gavel, Y.1    Von Heijne, G.2
  • 17
    • 0025765676 scopus 로고
    • Construction and characterization of a yeast artificial chromosome library of Arabidopsis which is suitable for chromosome walking
    • Grill, E., and Somerville, C. (1991). Construction and characterization of a yeast artificial chromosome library of Arabidopsis which is suitable for chromosome walking. Mol. Gen. Genet. 226, 484-490.
    • (1991) Mol. Gen. Genet. , vol.226 , pp. 484-490
    • Grill, E.1    Somerville, C.2
  • 18
    • 0003448569 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Harlow, E., and Lane, D. (1988). Antibodies: A Laboratory Manual. (Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press).
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 19
    • 0038671444 scopus 로고
    • Physical mapping of the Arabidopsis genome and its applications
    • R.G. Herrmann and B. Larkins, eds (New York: Plenum Press)
    • Hauge, B.M., Giraudat, J., Hanley, S., Hwang, I., Kohchi, T., and Goodman, H.M. (1991). Physical mapping of the Arabidopsis genome and its applications. In Plant Molecular Biology 2, R.G. Herrmann and B. Larkins, eds (New York: Plenum Press), pp. 239-248.
    • (1991) Plant Molecular Biology 2 , pp. 239-248
    • Hauge, B.M.1    Giraudat, J.2    Hanley, S.3    Hwang, I.4    Kohchi, T.5    Goodman, H.M.6
  • 22
    • 0027650566 scopus 로고
    • A procedure for mapping Arabidopsis mutations using co-dominant ecotype-specific PCR-based markers
    • Konieczny, A., and Ausubel, F.M. (1993). A procedure for mapping Arabidopsis mutations using co-dominant ecotype-specific PCR-based markers. Plant J. 4, 403-410.
    • (1993) Plant J. , vol.4 , pp. 403-410
    • Konieczny, A.1    Ausubel, F.M.2
  • 23
    • 0000811472 scopus 로고
    • Genetic control of light-inhibited hypocotyl elongation in Arabidopsis thaliana L
    • Koornneef, M., Rolff, E., and Spruit, C.J.P. (1980). Genetic control of light-inhibited hypocotyl elongation in Arabidopsis thaliana L. Heynh. Z. Pflanzenphysiol. 100, 147-160.
    • (1980) Heynh. Z. Pflanzenphysiol. , vol.100 , pp. 147-160
    • Koornneef, M.1    Rolff, E.2    Spruit, C.J.P.3
  • 24
    • 0000507396 scopus 로고
    • Self-assembly of synthetic phytochrome holoprotein in vitro
    • Lagarias, J.C., and Lagarias, D.M. (1989). Self-assembly of synthetic phytochrome holoprotein in vitro. Proc. Natl. Acad. Sci. USA 86, 5778-5780.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5778-5780
    • Lagarias, J.C.1    Lagarias, D.M.2
  • 25
    • 0000249480 scopus 로고
    • Chromopeptide from phytochrome. The structure and linkage of the Pr form of the phytochrome chromophore
    • Lagarias, J.C., and Rapoport, H. (1980). Chromopeptide from phytochrome. The structure and linkage of the Pr form of the phytochrome chromophore. J. Am. Chem. Soc. 102, 4821-4828.
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 4821-4828
    • Lagarias, J.C.1    Rapoport, H.2
  • 26
    • 0030087970 scopus 로고    scopus 로고
    • A jojoba β-ketoacyl-CoA synthase cDNA complements the canola fatty acid elongation mutation in transgenic plants
    • Lassner, M.W., Lardizabal, K., and Metz, J.G. (1996). A jojoba β-ketoacyl-CoA synthase cDNA complements the canola fatty acid elongation mutation in transgenic plants. Plant Cell 8, 281-292.
    • (1996) Plant Cell , vol.8 , pp. 281-292
    • Lassner, M.W.1    Lardizabal, K.2    Metz, J.G.3
  • 27
    • 0023943334 scopus 로고
    • Microassay of heme oxygenase by high-performance liquid chromatography: Application to assay of needle biopsies of human liver
    • Lincoln, B.C., Mayer, A., and Bonkovsky, H.L. (1988). Microassay of heme oxygenase by high-performance liquid chromatography: Application to assay of needle biopsies of human liver. Anal. Biochem. 170, 485-490.
    • (1988) Anal. Biochem. , vol.170 , pp. 485-490
    • Lincoln, B.C.1    Mayer, A.2    Bonkovsky, H.L.3
  • 28
    • 0025333899 scopus 로고
    • Molecular cloning and characterization of GPA1, a G protein a subunit gene from Arabidopsis thaliana
    • Ma, H., Yanofsky, M.F., and Meyerowitz, E.M. (1990). Molecular cloning and characterization of GPA1, a G protein a subunit gene from Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 87, 3821-3825.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3821-3825
    • Ma, H.1    Yanofsky, M.F.2    Meyerowitz, E.M.3
  • 29
    • 0030939106 scopus 로고    scopus 로고
    • Histidine-132 does not stabilize a distal water ligand and is not an important residue for the enzyme activity in heme oxygenase-1
    • Matera, K.M., Zhou, H., Migita, C.T., Hobert, S.E., Ishikawa, K., Katakura, K., Maeshima, H., Yoshida, T., and Ikeda-Saito, M. (1997). Histidine-132 does not stabilize a distal water ligand and is not an important residue for the enzyme activity in heme oxygenase-1. Biochemistry 36, 4909-4915.
    • (1997) Biochemistry , vol.36 , pp. 4909-4915
    • Matera, K.M.1    Zhou, H.2    Migita, C.T.3    Hobert, S.E.4    Ishikawa, K.5    Katakura, K.6    Maeshima, H.7    Yoshida, T.8    Ikeda-Saito, M.9
  • 30
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and bioassays with tobacco tissue culture
    • Murashige, T., and Skoog, F. (1962). A revised medium for rapid growth and bioassays with tobacco tissue culture. Physiol Plant. 15, 473-497.
    • (1962) Physiol Plant. , vol.15 , pp. 473-497
    • Murashige, T.1    Skoog, F.2
  • 31
    • 0000470601 scopus 로고
    • Isolation and initial characterization of Arabidopsis mutants that are deficient in phytochrome A
    • Nagatani, A., Reed, J.W., and Chory, J. (1993). Isolation and initial characterization of Arabidopsis mutants that are deficient in phytochrome A. Plant Physiol. 102, 269-277.
    • (1993) Plant Physiol. , vol.102 , pp. 269-277
    • Nagatani, A.1    Reed, J.W.2    Chory, J.3
  • 33
    • 0023691425 scopus 로고
    • Genetic applications of an inverse polymerase chain reaction
    • Ochman, H., Gerber, A.S., and Hartl, D.L. (1988). Genetic applications of an inverse polymerase chain reaction. Genetics 120, 621-623.
    • (1988) Genetics , vol.120 , pp. 621-623
    • Ochman, H.1    Gerber, A.S.2    Hartl, D.L.3
  • 34
    • 0026114515 scopus 로고
    • Blue light is required for survival of the tomato phytochrome-deficient aurea and the expression of four nuclear genes for plastidic proteins
    • Oelmüller, R., and Kendrick, R.E. (1991). Blue light is required for survival of the tomato phytochrome-deficient aurea and the expression of four nuclear genes for plastidic proteins. Plant Mol. Biol. 16, 293-299.
    • (1991) Plant Mol. Biol. , vol.16 , pp. 293-299
    • Oelmüller, R.1    Kendrick, R.E.2
  • 35
    • 0000115220 scopus 로고
    • Phytochrome-deficient hy1 and hy2 long hypocotyl mutants of Arabidopsis are defective in phytochrome chromophore biosynthesis
    • Parks, B.M., and Quail, P.M. (1991). Phytochrome-deficient hy1 and hy2 long hypocotyl mutants of Arabidopsis are defective in phytochrome chromophore biosynthesis. Plant Cell 3, 1177-1186.
    • (1991) Plant Cell , vol.3 , pp. 1177-1186
    • Parks, B.M.1    Quail, P.M.2
  • 36
    • 0011028739 scopus 로고
    • Assay of photomorphogenic photoreceptors
    • W.J. Shropshire and H. Mohr, eds (Berlin: Springer-Verlag)
    • Pratt, L.H. (1983). Assay of photomorphogenic photoreceptors. In Photomorphogenesis, W.J. Shropshire and H. Mohr, eds (Berlin: Springer-Verlag), pp. 152-177.
    • (1983) Photomorphogenesis , pp. 152-177
    • Pratt, L.H.1
  • 37
    • 0026355963 scopus 로고
    • Phytochrome: A light activated molecular switch that regulates plant gene expression
    • Quail, P.H. (1991). Phytochrome: A light activated molecular switch that regulates plant gene expression. Annu. Rev. Genet. 25, 389-409.
    • (1991) Annu. Rev. Genet. , vol.25 , pp. 389-409
    • Quail, P.H.1
  • 38
    • 0027949428 scopus 로고
    • Phytochrome A and phytochrome B have overlapping but distinct functions in Arabidopsis development
    • Reed, J.W., Nagatani, A., Elich, T.D., Fagan, M., and Chory, J. (1994). Phytochrome A and phytochrome B have overlapping but distinct functions in Arabidopsis development. Plant Physiol. 104, 1139-1149.
    • (1994) Plant Physiol. , vol.104 , pp. 1139-1149
    • Reed, J.W.1    Nagatani, A.2    Elich, T.D.3    Fagan, M.4    Chory, J.5
  • 39
    • 0026712223 scopus 로고
    • Biosynthesis of phycobilins: Ferredoxin-supported NADPH-independent heme oxygenase and phycobilin-forming activities from Cyanidium caldarium
    • Rhie, G., and Beale, S.I. (1992). Biosynthesis of phycobilins: Ferredoxin-supported NADPH-independent heme oxygenase and phycobilin-forming activities from Cyanidium caldarium. J. Biol. Chem. 267, 16088-16093.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16088-16093
    • Rhie, G.1    Beale, S.I.2
  • 40
    • 0029050375 scopus 로고
    • Phycobilin biosynthesis: Reductant requirements and product identification for heme oxygenase from Cyanidium caldarium
    • Rhie, G., and Beale, S.I. (1995). Phycobilin biosynthesis: Reductant requirements and product identification for heme oxygenase from Cyanidium caldarium. Arch. Biochem. Biophys. 320, 182-194.
    • (1995) Arch. Biochem. Biophys. , vol.320 , pp. 182-194
    • Rhie, G.1    Beale, S.I.2
  • 41
    • 0001954291 scopus 로고
    • Isolation and characterization of chloroplasts
    • C.H. Shaw, ed (Oxford: IRL Press)
    • Robinson, C., and Barnett, L.K. (1988). Isolation and characterization of chloroplasts. In Plant Molecular Biology: A Practical Approach, C.H. Shaw, ed (Oxford: IRL Press), pp. 67-78.
    • (1988) Plant Molecular Biology: A Practical Approach , pp. 67-78
    • Robinson, C.1    Barnett, L.K.2
  • 43
    • 0024760523 scopus 로고
    • Novel phytochrome sequences in Arabidopsis thaliana: Structure, evolution and differential expression of a plant regulatory photoreceptor family
    • Sharrock, R.A., and Quail, P.H. (1989). Novel phytochrome sequences in Arabidopsis thaliana: Structure, evolution and differential expression of a plant regulatory photoreceptor family. Genes Dev. 3, 1745-1757.
    • (1989) Genes Dev. , vol.3 , pp. 1745-1757
    • Sharrock, R.A.1    Quail, P.H.2
  • 44
    • 0028139567 scopus 로고
    • The induction of seed germination in Arabidopsis thaliana is regulated principally by phytochrome B and secondarily by phytochrome A
    • Shinomura, T., Nagatani, A., Chory, J., and Furuya, M. (1994). The induction of seed germination in Arabidopsis thaliana is regulated principally by phytochrome B and secondarily by phytochrome A. Plant Physiol. 104, 363-371.
    • (1994) Plant Physiol. , vol.104 , pp. 363-371
    • Shinomura, T.1    Nagatani, A.2    Chory, J.3    Furuya, M.4
  • 45
    • 0029839477 scopus 로고    scopus 로고
    • Action spectra for phytochrome A-and B-specific photoinduction of seed germination in Arabidopsis thaliana
    • Shinomura, T., Nagatani, A., Hanzawa, H., Kubota, M., Watanabe, M., and Furuya, M. (1996). Action spectra for phytochrome A-and B-specific photoinduction of seed germination in Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 93, 8129-8133.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8129-8133
    • Shinomura, T.1    Nagatani, A.2    Hanzawa, H.3    Kubota, M.4    Watanabe, M.5    Furuya, M.6
  • 46
    • 0028348843 scopus 로고
    • A general vector, pASK84, for cloning bacterial production, and single-step purification of antibody F-Ab fragments
    • Skerra, A. (1994). A general vector, pASK84, for cloning bacterial production, and single-step purification of antibody F-Ab fragments. Gene 141, 79-84.
    • (1994) Gene , vol.141 , pp. 79-84
    • Skerra, A.1
  • 47
    • 0028305713 scopus 로고
    • Isolation of a cDNA encoding chloroplast ferrochelatase from Arabidopsis thaliana by functional complementation of a yeast mutant
    • Smith, A.G., Santana, M.A., Wallace-Cook, A.D.M., Roper, J.M., and Labbe-Bois, R. (1994). Isolation of a cDNA encoding chloroplast ferrochelatase from Arabidopsis thaliana by functional complementation of a yeast mutant. J. Biol. Chem. 269, 13405-13413.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13405-13413
    • Smith, A.G.1    Santana, M.A.2    Wallace-Cook, A.D.M.3    Roper, J.M.4    Labbe-Bois, R.5
  • 48
    • 0028847505 scopus 로고
    • Physiological and ecological function within the phytochrome family
    • Smith, H. (1995). Physiological and ecological function within the phytochrome family. Annu. Rev. Plant Physiol. Plant Mol. Biol. 46, 289-315.
    • (1995) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.46 , pp. 289-315
    • Smith, H.1
  • 49
    • 0027985134 scopus 로고
    • Identification of histidine 25 as the heme ligand in human liver heme oxygenase
    • Sun, J., and Loehr, T.M. (1994). Identification of histidine 25 as the heme ligand in human liver heme oxygenase. Biochemistry 33, 13734-13740.
    • (1994) Biochemistry , vol.33 , pp. 13734-13740
    • Sun, J.1    Loehr, T.M.2
  • 50
    • 0027075178 scopus 로고
    • Nucleotide sequence of cDNA for porcine heme oxygenase and its expression in Escherichia coli
    • Suzuki, T., Sato, M., Ishikawa, K., and Yoshida, T. (1992). Nucleotide sequence of cDNA for porcine heme oxygenase and its expression in Escherichia coli. Biochem. Int. 28, 887-893.
    • (1992) Biochem. Int. , vol.28 , pp. 887-893
    • Suzuki, T.1    Sato, M.2    Ishikawa, K.3    Yoshida, T.4
  • 51
    • 0028057463 scopus 로고
    • Heme-heme oxygenase complex: Structure of the catalytic site and its implication for oxygen activation
    • Takahashi, S., Wang, J., Rousseau, D., Ishikawa, K., Yoshida, T., Host, J.R., and Ikeda-Saito, M. (1994a). Heme-heme oxygenase complex: structure of the catalytic site and its implication for oxygen activation. J. Biol. Chem. 269, 1010-1014.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1010-1014
    • Takahashi, S.1    Wang, J.2    Rousseau, D.3    Ishikawa, K.4    Yoshida, T.5    Host, J.R.6    Ikeda-Saito, M.7
  • 52
    • 0027947216 scopus 로고
    • Heme-heme oxygenase complex: Structure and properties of the catalytic site from resonance raman scattering
    • Takahashi, S., Wang, J., Rousseau, D., Ishikawa, K., Yoshida, T., Takeuchi, N., and Ikeda-Saito, M. (1994b). Heme-heme oxygenase complex: Structure and properties of the catalytic site from resonance raman scattering. Biochemistry 33, 5531-5538.
    • (1994) Biochemistry , vol.33 , pp. 5531-5538
    • Takahashi, S.1    Wang, J.2    Rousseau, D.3    Ishikawa, K.4    Yoshida, T.5    Takeuchi, N.6    Ikeda-Saito, M.7
  • 53
    • 0000582319 scopus 로고
    • Oxygen-bound heme-heme oxygenase complex: Evidence for a highly bent structure of the coordinated oxygen
    • Takahashi, S., Ishikawa, K., Takeuchi, N., Ikeda-Saito, M., Yoshida, T., and Rousseau, D. (1995). Oxygen-bound heme-heme oxygenase complex: Evidence for a highly bent structure of the coordinated oxygen. J. Am. Chem. Soc. 117, 6002-6006.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 6002-6006
    • Takahashi, S.1    Ishikawa, K.2    Takeuchi, N.3    Ikeda-Saito, M.4    Yoshida, T.5    Rousseau, D.6
  • 54
    • 0030978865 scopus 로고    scopus 로고
    • Phytochrome chromophore-deficient mutants
    • Terry, M.J. (1997). Phytochrome chromophore-deficient mutants. Plant Cell Environ. 20, 740-745.
    • (1997) Plant Cell Environ. , vol.20 , pp. 740-745
    • Terry, M.J.1
  • 55
    • 0029829904 scopus 로고    scopus 로고
    • The aurea and yellow-green-2 mutants of tomato are deficient in phytochrome chromophore synthesis
    • Terry, M.J., and Kendrick, R.E. (1996). The aurea and yellow-green-2 mutants of tomato are deficient in phytochrome chromophore synthesis. J. Biol. Chem. 271, 21681-21686.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21681-21686
    • Terry, M.J.1    Kendrick, R.E.2
  • 56
    • 0025788026 scopus 로고
    • Holophytochrome assembly. Coupled assay for phytochromobilin synthase in organello
    • Terry, M.J., and Lagarias, J.C. (1991). Holophytochrome assembly. Coupled assay for phytochromobilin synthase in organello. J. Biol. Chem. 266, 22215-22221.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22215-22221
    • Terry, M.J.1    Lagarias, J.C.2
  • 58
    • 0029064483 scopus 로고
    • (3Z)-and (3E)-Phytochromobilin are intermediates in the biosynthesis of the phytochrome chromophore
    • Terry, M.J., McDowell, M.T., and Lagarias, J.C. (1995). (3Z)-and (3E)-Phytochromobilin are intermediates in the biosynthesis of the phytochrome chromophore. J. Biol. Chem. 270, 11111-11118.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11111-11118
    • Terry, M.J.1    McDowell, M.T.2    Lagarias, J.C.3
  • 60
    • 85115107592 scopus 로고
    • Agrobacterium tumefeciens-mediated transformation of Arabidopsis thaliana root explants using kanamycin selection
    • Valvekens, D., Van Montagu, M., and Van Lijsebettens, M. (1988). Agrobacterium tumefeciens-mediated transformation of Arabidopsis thaliana root explants using kanamycin selection. Proc. Natl. Acad. Sci. USA 85, 5536-5540.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5536-5540
    • Valvekens, D.1    Van Montagu, M.2    Van Lijsebettens, M.3
  • 62
    • 0024542834 scopus 로고
    • Domain structure of mitochondrial and chloroplast targeting peptides
    • von Heijne, G., Steppuhn, J., and Herrmann, R.G. (1989). Domain structure of mitochondrial and chloroplast targeting peptides. Eur. J. Biochem. 180, 535-545.
    • (1989) Eur. J. Biochem. , vol.180 , pp. 535-545
    • Von Heijne, G.1    Steppuhn, J.2    Herrmann, R.G.3
  • 63
    • 0025413451 scopus 로고
    • Isolation of single-copy-sequence clones from a yeast artificial chromosome library of randomly-sheared Arabidopsis thaliana DNA
    • Ward, E.R., and Jen, G.C. (1990). Isolation of single-copy-sequence clones from a yeast artificial chromosome library of randomly-sheared Arabidopsis thaliana DNA. Plant Mol. Biol. 14, 561-568.
    • (1990) Plant Mol. Biol. , vol.14 , pp. 561-568
    • Ward, E.R.1    Jen, G.C.2
  • 64
    • 0030027077 scopus 로고    scopus 로고
    • The phytochrome-deficient pcd1 mutant of pea is unable to convert heme to biliverdin IXa
    • Weller, J.L., Terry, M.J., Rameau, C., Reid, J.B., and Kendrick, R.E. (1996). The phytochrome-deficient pcd1 mutant of pea is unable to convert heme to biliverdin IXa. Plant Cell 8, 55-67.
    • (1996) Plant Cell , vol.8 , pp. 55-67
    • Weller, J.L.1    Terry, M.J.2    Rameau, C.3    Reid, J.B.4    Kendrick, R.E.5
  • 65
    • 0030742733 scopus 로고    scopus 로고
    • The phytochrome-deficient pcd2 mutant of pea is unable to convert biliverdin IXa to 3(Z)-phytochromobilin
    • Weller, J.L., Terry, M.J., Reid, J.B., and Kendrick, R.E. (1997). The phytochrome-deficient pcd2 mutant of pea is unable to convert biliverdin IXa to 3(Z)-phytochromobilin. Plant J. 11, 1177-1186.
    • (1997) Plant J. , vol.11 , pp. 1177-1186
    • Weller, J.L.1    Terry, M.J.2    Reid, J.B.3    Kendrick, R.E.4
  • 67
    • 0025739047 scopus 로고
    • Degradation of heme by a soluble peptide of heme oxygenase obtained from rat liver microsomes by mild trypsinization
    • Yoshida, T., Ishikawa, K., and Sato, M. (1991). Degradation of heme by a soluble peptide of heme oxygenase obtained from rat liver microsomes by mild trypsinization. Eur. J. Biochem. 199, 729-733.
    • (1991) Eur. J. Biochem. , vol.199 , pp. 729-733
    • Yoshida, T.1    Ishikawa, K.2    Sato, M.3


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