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Volumn 20, Issue 6, 1997, Pages 657-665

An emerging molecular map of the phytochromes

Author keywords

Functional domains; Histidine kinase; Photo sensory perception; Phytochromes; Signal transduction; Structural domains; Structure function relationships; Two component systems

Indexed keywords

CYANOBACTERIA; SYNECHOCYSTIS;

EID: 0030994224     PISSN: 01407791     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-3040.1997.d01-108.x     Document Type: Article
Times cited : (133)

References (60)
  • 1
    • 0025885497 scopus 로고
    • Phytochrome a overexpression inhibits hypocotyl elongation in transgenic Arabidopsis
    • Boylan M.T. & Quail P.H. (1991) Phytochrome A overexpression inhibits hypocotyl elongation in transgenic Arabidopsis. Proceedings of the National Academy of Sciences USA 88, 10806-10810.
    • (1991) Proceedings of the National Academy of Sciences USA , vol.88 , pp. 10806-10810
    • Boylan, M.T.1    Quail, P.H.2
  • 2
    • 0028385768 scopus 로고
    • Dominant negative suppression of Arabidopsis photoresponses by mutant phytochrome a sequences identifies spatially discrete regulatory domains in the photoreceptor
    • Boylan M., Douglas N. & Quail P.H. (1994) Dominant negative suppression of Arabidopsis photoresponses by mutant phytochrome A sequences identifies spatially discrete regulatory domains in the photoreceptor. Plant Cell 6, 449-460.
    • (1994) Plant Cell , vol.6 , pp. 449-460
    • Boylan, M.1    Douglas, N.2    Quail, P.H.3
  • 3
    • 0030473678 scopus 로고    scopus 로고
    • Are the phytochromes protein kinases?
    • Boylan M.T. & Quail P.H. (1996) Are the phytochromes protein kinases? Protoplasma 195, 59-67.
    • (1996) Protoplasma , vol.195 , pp. 59-67
    • Boylan, M.T.1    Quail, P.H.2
  • 4
    • 0001755043 scopus 로고
    • The use of transgenic plants to examine phytochrome structure/function
    • (eds R. E. Kendrick & G. H. M. Kronenberg), Kluwer, Dordrecht, The Netherlands
    • Cherry J.R. & Vierstra R.D. (1994) The use of transgenic plants to examine phytochrome structure/function. In Photomorphogenesis in Plants, 2nd edn (eds R. E. Kendrick & G. H. M. Kronenberg), pp. 271-300. Kluwer, Dordrecht, The Netherlands.
    • (1994) Photomorphogenesis in Plants, 2nd Edn , pp. 271-300
    • Cherry, J.R.1    Vierstra, R.D.2
  • 6
    • 0027597621 scopus 로고
    • Carboxy-terminal deletion analysis of oat phytochrome a reveals the presence of separate domains required for structure and biological activity
    • Cherry J.R., Hondred D., Walker J.M, Keller J.M., Hershey H.P. & Vierstra R.D. (1993) Carboxy-terminal deletion analysis of oat phytochrome A reveals the presence of separate domains required for structure and biological activity. Plant Cell 5, 565-575.
    • (1993) Plant Cell , vol.5 , pp. 565-575
    • Cherry, J.R.1    Hondred, D.2    Walker, J.M.3    Keller, J.M.4    Hershey, H.P.5    Vierstra, R.D.6
  • 7
    • 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. & Sharrock R.A. (1994) The phytochrome apoprotein family in Arabidopsis is encoded by five genes: The sequences and expression of PHYD and PHYE. Plant Molecular Biology 25, 413-427.
    • (1994) Plant Molecular Biology , vol.25 , pp. 413-427
    • Clack, T.1    Mathews, S.2    Sharrock, R.A.3
  • 9
    • 0026729104 scopus 로고
    • Phytochome assembly: The structure and biological activity of 2 (R), 3 (E)-phytochromobilin derived from phycobiliproteins
    • Cornejo J., Beale S.I., Terry M.J. & Lagarias J.C. (1992) Phytochome assembly: the structure and biological activity of 2 (R), 3 (E)-phytochromobilin derived from phycobiliproteins. Journal of Biological Chemistry 267, 14790-14798.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 14790-14798
    • Cornejo, J.1    Beale, S.I.2    Terry, M.J.3    Lagarias, J.C.4
  • 12
    • 0027759656 scopus 로고
    • Mutational analysis of the pea phytochrome a chromophore pocket: Chromophore assembly with apophytochrome a and photoreversibility
    • Deforce L., Furuya M. & Song P.S. (1993) Mutational analysis of the pea phytochrome A chromophore pocket: chromophore assembly with apophytochrome A and photoreversibility. Biochemistry 32, 14165-14172.
    • (1993) Biochemistry , vol.32 , pp. 14165-14172
    • Deforce, L.1    Furuya, M.2    Song, P.S.3
  • 13
    • 0026812466 scopus 로고
    • Localization of protein-protein interactions between subunits of phytochrome
    • Edgerton M.D. & Jones A.M. (1992) Localization of protein-protein interactions between subunits of phytochrome. Plant Cell 4, 161-171.
    • (1992) Plant Cell , vol.4 , pp. 161-171
    • Edgerton, M.D.1    Jones, A.M.2
  • 14
    • 0027291961 scopus 로고
    • Subunit interactions in the carboxy-terminal domain of phytochrome
    • Edgerton M.D. & Jones A.M. (1993) Subunit interactions in the carboxy-terminal domain of phytochrome. Biochemistry 32, 8239-8245.
    • (1993) Biochemistry , vol.32 , pp. 8239-8245
    • Edgerton, M.D.1    Jones, A.M.2
  • 15
    • 0002237440 scopus 로고
    • Assembly and properties of holophytochrome
    • (eds R. E. Kendrick & G. H. M. Kronenberg), Kluwer, Dordrecht, The Netherlands
    • Furuya M. & Song P.S. (1994) Assembly and properties of holophytochrome. In Photomorphogenesis in Plants, 2nd edn (eds R. E. Kendrick & G. H. M. Kronenberg), pp. 105-140. Kluwer, Dordrecht, The Netherlands.
    • (1994) Photomorphogenesis in Plants, 2nd Edn , pp. 105-140
    • Furuya, M.1    Song, P.S.2
  • 16
    • 0001672383 scopus 로고
    • Sequence analysis of proteolytic fragments of 124-kilodalton phytochrome from etiolated Avena sativa L.: Conclusions on the conformation of the native protein
    • Grimm R., Eckerskorn C., Lottspeich F., Zenger C. & Rüdiger W. (1988) Sequence analysis of proteolytic fragments of 124-kilodalton phytochrome from etiolated Avena sativa L.: Conclusions on the conformation of the native protein. Planta 174, 396-401.
    • (1988) Planta , vol.174 , pp. 396-401
    • Grimm, R.1    Eckerskorn, C.2    Lottspeich, F.3    Zenger, C.4    Rüdiger, W.5
  • 17
    • 0000808204 scopus 로고
    • Quaternary structure of 124 kiloDalton phytochrome from Avena sativa
    • Jones A.M. & Quail P.H. (1986) Quaternary structure of 124 kiloDalton phytochrome from Avena sativa. Biochemistry 25, 2987-2995.
    • (1986) Biochemistry , vol.25 , pp. 2987-2995
    • Jones, A.M.1    Quail, P.H.2
  • 18
    • 0024652229 scopus 로고
    • Domain structure of phytochrome from Avena sativa visualized by electron microscopy
    • Jones A.M. & Erickson H.P. (1989) Domain structure of phytochrome from Avena sativa visualized by electron microscopy. Photochemistry and Photobiology 49, 479-483.
    • (1989) Photochemistry and Photobiology , vol.49 , pp. 479-483
    • Jones, A.M.1    Erickson, H.P.2
  • 19
    • 0000032449 scopus 로고
    • The roles of separate molecular domains in the structure of phytochrome from Avena sativa L
    • Jones A.M., Vierstra R.D., Daniels S.M. & Quail P.H. (1985) The roles of separate molecular domains in the structure of phytochrome from Avena sativa L. Planta 164, 501-506.
    • (1985) Planta , vol.164 , pp. 501-506
    • Jones, A.M.1    Vierstra, R.D.2    Daniels, S.M.3    Quail, P.H.4
  • 20
    • 0030087691 scopus 로고
    • The amino-terminus of phytochrome a contains two distinct functional domains
    • Jordan E.T., Cherry J.R., Walker J.M. & Vierstra R.D. (1995) The amino-terminus of phytochrome A contains two distinct functional domains. The Plant Journal 9, 243-257.
    • (1995) The Plant Journal , vol.9 , pp. 243-257
    • Jordan, E.T.1    Cherry, J.R.2    Walker, J.M.3    Vierstra, R.D.4
  • 22
    • 0029818880 scopus 로고    scopus 로고
    • Similarity of a chromatic adaptation sensor to phytochrome and ethylene receptors
    • Kehoe D.M. & Grossman A.R. (1996) Similarity of a chromatic adaptation sensor to phytochrome and ethylene receptors. Science 273, 1409-1411.
    • (1996) Science , vol.273 , pp. 1409-1411
    • Kehoe, D.M.1    Grossman, A.R.2
  • 27
    • 0029582690 scopus 로고
    • Atypical phytochrome gene structure in the green alga Mesotaenium caldariorum
    • Lagarias D.M. Wu, S.-H. & Lagarias J.C. (1995) Atypical phytochrome gene structure in the green alga Mesotaenium caldariorum. Plant Molecular Biology 29, 1127-1142.
    • (1995) Plant Molecular Biology , vol.29 , pp. 1127-1142
    • Lagarias, D.M.1    Wu, S.-H.2    Lagarias, J.C.3
  • 28
    • 0028566686 scopus 로고
    • Phytochrome assembly in living cells of the yeast Saccaromyces cerevisiae
    • Li L. & Lagarias J.C. (1994) Phytochrome assembly in living cells of the yeast Saccaromyces cerevisiae. Proceedings of the National Academy of Sciences USA 91, 12535-12539.
    • (1994) Proceedings of the National Academy of Sciences USA , vol.91 , pp. 12535-12539
    • Li, L.1    Lagarias, J.C.2
  • 30
    • 0025269459 scopus 로고
    • Phosphopeptide mapping of Avena phytochrome phosphorylated by protein kinases in vitro
    • McMichael R.W., Jr & Lagarias J.C. (1990b) Phosphopeptide mapping of Avena phytochrome phosphorylated by protein kinases in vitro. Biochemistry 29, 3872-3878.
    • (1990) Biochemistry , vol.29 , pp. 3872-3878
    • McMichael Jr., R.W.1    Lagarias, J.C.2
  • 31
    • 0001372273 scopus 로고
    • Evolution of the phytochrome gene family and its utility for phylogenetic analyses of angiosperms
    • Mathews S., Lavin M. & Sharrock R.A. (1995) Evolution of the phytochrome gene family and its utility for phylogenetic analyses of angiosperms. Annals of the Missouri Botanical Garden 82, 296-321.
    • (1995) Annals of the Missouri Botanical Garden , vol.82 , pp. 296-321
    • Mathews, S.1    Lavin, M.2    Sharrock, R.A.3
  • 32
    • 0027056677 scopus 로고
    • Communication modules in bacterial signaling proteins
    • Parkinson J.S. & Kofoid E.C. (1992) Communication modules in bacterial signaling proteins. Annual Reviews of Genetics 26, 71-112.
    • (1992) Annual Reviews of Genetics , vol.26 , pp. 71-112
    • Parkinson, J.S.1    Kofoid, E.C.2
  • 33
    • 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. Annual Reviews of Genetics 25, 389-409.
    • (1991) Annual Reviews of Genetics , vol.25 , pp. 389-409
    • Quail, P.H.1
  • 34
    • 0031194090 scopus 로고    scopus 로고
    • The phytochromes: A biochemical mechanism of action in site?
    • in press
    • Quail P.H. (1997) The phytochromes: A biochemical mechanism of action in site? BioEssays, in press.
    • (1997) BioEssays
    • Quail, P.H.1
  • 37
    • 0025875671 scopus 로고
    • Natural substrates of the ubiquitin proteolytic pathway
    • Rechsteiner M. (1991) Natural substrates of the ubiquitin proteolytic pathway. Cell 66, 615-618.
    • (1991) Cell , vol.66 , pp. 615-618
    • Rechsteiner, M.1
  • 38
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • Rogers S., Wells R. & Rechsteiner M. (1986) Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 234, 364-368.
    • (1986) Science , vol.234 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 39
    • 0026947843 scopus 로고
    • Signal transduction by phytochrome: Phytochromes have a module related to the transmitter modules of bacterial sensor proteins
    • Schneider-Poetsch H.A.W. (1992) Signal transduction by phytochrome: phytochromes have a module related to the transmitter modules of bacterial sensor proteins. Photochemistry and Photobiology 56, 839-846.
    • (1992) Photochemistry and Photobiology , vol.56 , pp. 839-846
    • Schneider-Poetsch, H.A.W.1
  • 40
    • 0009853585 scopus 로고
    • Proposal on the nature of phytochrome action based on the C-terminal sequences of phytochrome
    • Schneider-Poetsch H.A.W. & Braun B. (1991) Proposal on the nature of phytochrome action based on the C-terminal sequences of phytochrome. Journal of Plant Physiology 137, 576-580.
    • (1991) Journal of Plant Physiology , vol.137 , pp. 576-580
    • Schneider-Poetsch, H.A.W.1    Braun, B.2
  • 41
    • 0025970168 scopus 로고
    • Phytochromes and bacterial sensor proteins are related by structural and functional homologies
    • Schneider-Poetsch H.A.W., Braun B., Marx S. & Schaumburg A. (1991) Phytochromes and bacterial sensor proteins are related by structural and functional homologies. FEBS Journal 281, 245-249.
    • (1991) FEBS Journal , vol.281 , pp. 245-249
    • Schneider-Poetsch, H.A.W.1    Braun, B.2    Marx, S.3    Schaumburg, A.4
  • 42
    • 0031153908 scopus 로고    scopus 로고
    • Antagonistic but complementary actions of phytochromes a and B allow optimum seedling de-etiolation
    • in press
    • Smith H. Xu Y. & Quail P.H. (1997) Antagonistic but complementary actions of phytochromes A and B allow optimum seedling de-etiolation. Plant Physiology, in press.
    • (1997) Plant Physiology
    • Smith, H.1    Xu, Y.2    Quail, P.H.3
  • 43
    • 0000726631 scopus 로고
    • The hy3 long hypocotyl mutant of Arabidopsis is deficient in phytochrome B
    • Somers D.E., Sharrock R.A., Tepperman J.M. & Quail P.H. (1991) The hy3 long hypocotyl mutant of Arabidopsis is deficient in phytochrome B. Plant Cell 3, 1263-1274.
    • (1991) Plant Cell , vol.3 , pp. 1263-1274
    • Somers, D.E.1    Sharrock, R.A.2    Tepperman, J.M.3    Quail, P.H.4
  • 44
    • 0348017860 scopus 로고
    • Phytochrome as a light switch for gene expression in plants
    • Song, P.-S. (1993) Phytochrome as a light switch for gene expression in plants. Molecules and Cells 3, 353-361.
    • (1993) Molecules and Cells , vol.3 , pp. 353-361
    • Song, P.-S.1
  • 45
  • 46
    • 0027062967 scopus 로고
    • Serine-to-alanine substitutions at the amino-terminal region of phytochrome a result in an increase in biological activity
    • Stockhaus J., Nagatani A., Halfter U. Kay S., Furuya M. & Chua, N.-H. (1992) Serine-to-alanine substitutions at the amino-terminal region of phytochrome A result in an increase in biological activity. Genes and Development 6, 2364-2372.
    • (1992) Genes and Development , vol.6 , pp. 2364-2372
    • Stockhaus, J.1    Nagatani, A.2    Halfter, U.3    Kay, S.4    Furuya, M.5    Chua, N.-H.6
  • 47
    • 0027219557 scopus 로고
    • Intrinsic activity of the Lin-12 and Notch intracellular domains in vivo
    • Struhl G., Fitzgerald K. & Greenwald I. (1993) Intrinsic activity of the Lin-12 and Notch intracellular domains in vivo. Cell 74, 331-345.
    • (1993) Cell , vol.74 , pp. 331-345
    • Struhl, G.1    Fitzgerald, K.2    Greenwald, I.3
  • 49
    • 0027135080 scopus 로고
    • Illuminating phytochrome functions - There is light at the end of the tunnel
    • Vierstra R.D. (1993) Illuminating phytochrome functions - There is light at the end of the tunnel. Plant Physiology 103, 679-684.
    • (1993) Plant Physiology , vol.103 , pp. 679-684
    • Vierstra, R.D.1
  • 50
    • 0001906410 scopus 로고
    • Phytochrome degradation
    • (eds R. E. Kendrick & G. H. M. Kronenberg), Kluwer, Dordrecht
    • Vierstra R.D. (1994) Phytochrome degradation. In Photomorphogenesis in Plants, 2nd edn (eds R. E. Kendrick & G. H. M. Kronenberg), pp. 141-162. Kluwer, Dordrecht.
    • (1994) Photomorphogenesis in Plants, 2nd Edn , pp. 141-162
    • Vierstra, R.D.1
  • 51
    • 0030267548 scopus 로고    scopus 로고
    • Proteolysis in plants: Mechanisms and functions
    • Vierstra R.D. (1996) Proteolysis in plants: mechanisms and functions. Plant Molecular Biology 32, 275-302.
    • (1996) Plant Molecular Biology , vol.32 , pp. 275-302
    • Vierstra, R.D.1
  • 52
    • 0039642860 scopus 로고
    • Phytochrome: The protein
    • (eds R. E. Kendrick & G. H. M. Kronenberg), Martinus Nijhoff, Dordrecht
    • Vierstra R.D. & Quail P.H. (1986) Phytochrome: the protein. In Photomorphogenesis in Plants (eds R. E. Kendrick & G. H. M. Kronenberg), pp. 35-60. Martinus Nijhoff, Dordrecht.
    • (1986) Photomorphogenesis in Plants , pp. 35-60
    • Vierstra, R.D.1    Quail, P.H.2
  • 53
    • 0029021892 scopus 로고
    • Mutational analysis of phytochrome B identifies a small COOH-terminal-domain region critical for regulatory activity
    • Wagner D. & Quail P.H. (1995) Mutational analysis of phytochrome B identifies a small COOH-terminal-domain region critical for regulatory activity. Proceedings of the National Academy of Sciences USA 92, 8596-8600.
    • (1995) Proceedings of the National Academy of Sciences USA , vol.92 , pp. 8596-8600
    • Wagner, D.1    Quail, P.H.2
  • 54
    • 0001506628 scopus 로고    scopus 로고
    • Two small spatially distinct regions of phytochrome B are required for efficient signaling rates
    • Wagner D., Koloszvari M. & Quail P.H. (1996a) Two small spatially distinct regions of phytochrome B are required for efficient signaling rates. Plant Cell 8, 859-871.
    • (1996) Plant Cell , vol.8 , pp. 859-871
    • Wagner, D.1    Koloszvari, M.2    Quail, P.H.3
  • 55
    • 0029664315 scopus 로고    scopus 로고
    • Chromophore-bearing NHsub 2-terminal domains of phytochromes a and B determine their photosensory specificity and differential light lability
    • Wagner D., Fairchild C.D., Kuhn R.M. & Quail P.H. (1996b) Chromophore-bearing NHsub 2-terminal domains of phytochromes A and B determine their photosensory specificity and differential light lability. Proceedings of the National Academy of Sciences USA 93, 4011-4015.
    • (1996) Proceedings of the National Academy of Sciences USA , vol.93 , pp. 4011-4015
    • Wagner, D.1    Fairchild, C.D.2    Kuhn, R.M.3    Quail, P.H.4
  • 56
    • 0031131584 scopus 로고    scopus 로고
    • RED1 is necessary for phytochrome B-mediated red light specific signal transduction in Arabidopsis
    • in press
    • Wagner D., Hoecker E. & Quail P.H. (1997) RED1 is necessary for phytochrome B-mediated red light specific signal transduction in Arabidopsis. Plant Cell, in press.
    • (1997) Plant Cell
    • Wagner, D.1    Hoecker, E.2    Quail, P.H.3
  • 58
    • 0030294725 scopus 로고    scopus 로고
    • Phytochrome of the green alga Mougeotia: CDNA sequence, autoregulaiton and phylogenetic position
    • Winands A. & Wagner G. (1996) Phytochrome of the green alga Mougeotia: cDNA sequence, autoregulaiton and phylogenetic position. Plant Molecular Biology 32, 589-597.
    • (1996) Plant Molecular Biology , vol.32 , pp. 589-597
    • Winands, A.1    Wagner, G.2
  • 59
    • 0023050293 scopus 로고
    • Phosphorylation of Avena Phytochrome in Vitro as a Probe of Light-Induced Conformational Changes
    • Wong, Y.-S., Cheng, H.-C., Walsh D.A. & Lagarias J.C. (1986) Phosphorylation of Avena Phytochrome in Vitro as a Probe of Light-Induced Conformational Changes. Journal of Biological Chemistry 261, 12089-12097.
    • (1986) Journal of Biological Chemistry , vol.261 , pp. 12089-12097
    • Wong, Y.-S.1    Cheng, H.-C.2    Walsh, D.A.3    Lagarias, J.C.4
  • 60
    • 0029360558 scopus 로고
    • Missense mutations define a restricted segment in the COOH-terminal domain of phytochrome a critical to its regulatory activity
    • Xu Y., Parks B.M., Short T.W. & Quail P.H. (1995) Missense mutations define a restricted segment in the COOH-terminal domain of phytochrome A critical to its regulatory activity. Plant Cell 7, 1433-1443.
    • (1995) Plant Cell , vol.7 , pp. 1433-1443
    • Xu, Y.1    Parks, B.M.2    Short, T.W.3    Quail, P.H.4


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