메뉴 건너뛰기




Volumn , Issue , 2002, Pages 273-295

Cyanophytochromes, Bacteriophytochromes, and Plant Phytochromes. Light-Regulated Kinases Related to Bacterial Two-Component Regulators

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CHROMOPHORES; PHOTOCHROMISM; PLANTS (BOTANY); SIGNAL TRANSDUCTION; VISION;

EID: 84902412814     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-012372484-7/50014-X     Document Type: Chapter
Times cited : (9)

References (64)
  • 1
    • 0034131527 scopus 로고    scopus 로고
    • Light: An indicator of time and place
    • Neff M.M., Fankhauser C., Chory J. Light: An indicator of time and place. Genes Dev. 2000, 14:257-271.
    • (2000) Genes Dev. , vol.14 , pp. 257-271
    • Neff, M.M.1    Fankhauser, C.2    Chory, J.3
  • 4
    • 0034609795 scopus 로고    scopus 로고
    • Phytochromes and light signal perception by plants: An emerging synthesis
    • Smith H. Phytochromes and light signal perception by plants: An emerging synthesis. Nature 2000, 407:585-591.
    • (2000) Nature , vol.407 , pp. 585-591
    • Smith, H.1
  • 7
    • 0034619430 scopus 로고    scopus 로고
    • Defining the bilin lyase domain: Lessons from the extended phytochrome superfamily
    • Wu S.H., Lagarias J.C. Defining the bilin lyase domain: Lessons from the extended phytochrome superfamily. Biochemistry 2000, 39:13487-13495.
    • (2000) Biochemistry , vol.39 , pp. 13487-13495
    • Wu, S.H.1    Lagarias, J.C.2
  • 8
    • 0032991822 scopus 로고    scopus 로고
    • The Arabidopsis thaliana HY1 locus, required for phytochrome-chromophore biosynthesis, encodes a protein related to heme oxygenases
    • Davis S.J., Kurepa J., Vierstra R.D. The Arabidopsis thaliana HY1 locus, required for phytochrome-chromophore biosynthesis, encodes a protein related to heme oxygenases. Proc. Natl. Acad. Sci. USA 1999, 96:6541-6546.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6541-6546
    • Davis, S.J.1    Kurepa, J.2    Vierstra, R.D.3
  • 9
    • 0030978865 scopus 로고    scopus 로고
    • Phytochrome deficient mutants
    • Terry M.L. Phytochrome deficient mutants. Plant Cell Environ 1997, 20:740-745.
    • (1997) Plant Cell Environ , vol.20 , pp. 740-745
    • Terry, M.L.1
  • 10
    • 0030957915 scopus 로고    scopus 로고
    • Roles of different phytochromes in Arabidopsis morphogenesis
    • Whitelam G.C., Devlin P.F. Roles of different phytochromes in Arabidopsis morphogenesis. Plant Cell Environ. 1997, 20:752-758.
    • (1997) Plant Cell Environ. , vol.20 , pp. 752-758
    • Whitelam, G.C.1    Devlin, P.F.2
  • 11
    • 0032925887 scopus 로고    scopus 로고
    • Mass spectrometric characterization of oat phytochrome A: Isoforms and post-translational modifications
    • Lapko V.N., Jiang X.Y., Smith D.L., Song P.S. Mass spectrometric characterization of oat phytochrome A: Isoforms and post-translational modifications. Protein Sci. 1999, 8:1032-1044.
    • (1999) Protein Sci. , vol.8 , pp. 1032-1044
    • Lapko, V.N.1    Jiang, X.Y.2    Smith, D.L.3    Song, P.S.4
  • 12
    • 0030994224 scopus 로고    scopus 로고
    • An emerging molecular map of phytochromes
    • Quail P.H. An emerging molecular map of phytochromes. Plant Cell Environ. 1997, 20:657-665.
    • (1997) Plant Cell Environ. , vol.20 , pp. 657-665
    • Quail, P.H.1
  • 13
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: Internal sensors of oxygen, redox potential, and light
    • Taylor B.L., Zhulin I.B. PAS domains: Internal sensors of oxygen, redox potential, and light. Microbiol. Mol. Biol. Rev. 1999, 63:1051-1058.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 1051-1058
    • Taylor, B.L.1    Zhulin, I.B.2
  • 14
    • 0019330566 scopus 로고
    • Partial characterization of undegraded oat phytochrome
    • Hunt R.E., Pratt L.H. Partial characterization of undegraded oat phytochrome. Biochemistry 1980, 19:390-394.
    • (1980) Biochemistry , vol.19 , pp. 390-394
    • Hunt, R.E.1    Pratt, L.H.2
  • 15
    • 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. Phosphorylation of Avena phytochrome in vitro as a probe of light-induced conformational changes. J. Biol. Chem. 1986, 261:12089-12097.
    • (1986) J. Biol. Chem. , vol.261 , pp. 12089-12097
    • Wong, Y.S.1    Cheng, H.C.2    Walsh, D.A.3    Lagarias, J.C.4
  • 16
    • 0343875544 scopus 로고
    • Affinity labeling of Avena phytochrome with ATP analogs
    • Wong Y.S., Lagarias J.C. Affinity labeling of Avena phytochrome with ATP analogs. Proc. Natl. Acad. Sci. USA 1989, 86:3469-3473.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 3469-3473
    • Wong, Y.S.1    Lagarias, J.C.2
  • 17
    • 0028084131 scopus 로고
    • Pr-specific phytochrome phosphorylation in vitro by a protein kinase present in anti-phytochrome maize immunoprecipitates
    • Biermann B.J., Pao L.I., Feldman L.J. Pr-specific phytochrome phosphorylation in vitro by a protein kinase present in anti-phytochrome maize immunoprecipitates. Plant Physiol. 1994, 105:243-251.
    • (1994) Plant Physiol. , vol.105 , pp. 243-251
    • Biermann, B.J.1    Pao, L.I.2    Feldman, L.J.3
  • 18
    • 0031454154 scopus 로고    scopus 로고
    • Phytochrome: If it looks and smells like a histidine kinase, is it a histidine kinase?
    • Elich T.D., Chory J. Phytochrome: If it looks and smells like a histidine kinase, is it a histidine kinase?. Cell 1997, 91:713-716.
    • (1997) Cell , vol.91 , pp. 713-716
    • Elich, T.D.1    Chory, J.2
  • 19
    • 0007238824 scopus 로고    scopus 로고
    • Phytochrome autophosphorylation: No longer a red/far red herring?
    • Reed J.W. Phytochrome autophosphorylation: No longer a red/far red herring?. Trends Plant Sci. 1998, 3:43-44.
    • (1998) Trends Plant Sci. , vol.3 , pp. 43-44
    • Reed, J.W.1
  • 20
    • 0026947843 scopus 로고
    • Signal transduction by phytochrome: Phytochromes have a module related to the transmitter modules of bacterial sensor proteins
    • Schneider-Poetsch H.A. Signal transduction by phytochrome: Phytochromes have a module related to the transmitter modules of bacterial sensor proteins. Photochem. Photobiol. 1992, 56:839-846.
    • (1992) Photochem. Photobiol. , vol.56 , pp. 839-846
    • Schneider-Poetsch, H.A.1
  • 21
    • 0030595328 scopus 로고    scopus 로고
    • Signal transduction via the multistep phosphorelay: Not necessarily the road less traveled
    • Appleby J.L., Parkinson J.S., Bourret R.B. Signal transduction via the multistep phosphorelay: Not necessarily the road less traveled. Cell 1996, 86:845-848.
    • (1996) Cell , vol.86 , pp. 845-848
    • Appleby, J.L.1    Parkinson, J.S.2    Bourret, R.B.3
  • 23
    • 0027380220 scopus 로고
    • Arabidopsis ethylene-response gene ETR1: Similarity of product to two-component regulators
    • Chang C., Kwok S.F., Bleecker A.B., Meyerowitz E.M. Arabidopsis ethylene-response gene ETR1: Similarity of product to two-component regulators. Science 1993, 262:539-544.
    • (1993) Science , vol.262 , pp. 539-544
    • Chang, C.1    Kwok, S.F.2    Bleecker, A.B.3    Meyerowitz, E.M.4
  • 24
    • 0030575903 scopus 로고    scopus 로고
    • CKI1, a Histidine kinase homolog implicated in cytokinin signal transduction
    • Kakimoto T. CKI1, a Histidine kinase homolog implicated in cytokinin signal transduction. Science 1996, 274:982-985.
    • (1996) Science , vol.274 , pp. 982-985
    • Kakimoto, T.1
  • 25
    • 0032506138 scopus 로고    scopus 로고
    • Eukaryotic phytochromes: light-regulated serine/threonine protein kinases with histidine kinase ancestry
    • Yeh K.C., Lagarias J.C. Eukaryotic phytochromes: light-regulated serine/threonine protein kinases with histidine kinase ancestry. Proc. Natl. Acad. Sci. USA 1998, 95:13976-13981.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13976-13981
    • Yeh, K.C.1    Lagarias, J.C.2
  • 26
    • 0030473678 scopus 로고    scopus 로고
    • Are phytochromes protein kinases?
    • Boylan M.T., Quail P.H. Are phytochromes protein kinases?. Protoplasma 1996, 195:59-67.
    • (1996) Protoplasma , vol.195 , pp. 59-67
    • Boylan, M.T.1    Quail, P.H.2
  • 27
    • 0034608882 scopus 로고    scopus 로고
    • The histidine kinase-related domain participates in phytochrome B function but is dispensable
    • Krall L., Reed J.W. The histidine kinase-related domain participates in phytochrome B function but is dispensable. Proc. Natl. Acad. Sci. USA 2000, 97:8169-8174.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8169-8174
    • Krall, L.1    Reed, J.W.2
  • 28
    • 0029046676 scopus 로고
    • Divergence of the phytochrome gene Family predates angiosperm evolution and suggests that Selaginella and Equisetum arose prior to Psilotum
    • Kolukisaoglu H.U., Marx S., Wiegmann C., Hanelt S., Schneider-Poetsch H.A. Divergence of the phytochrome gene Family predates angiosperm evolution and suggests that Selaginella and Equisetum arose prior to Psilotum. J. Mol. Evol. 1995, 41:329-337.
    • (1995) J. Mol. Evol. , vol.41 , pp. 329-337
    • Kolukisaoglu, H.U.1    Marx, S.2    Wiegmann, C.3    Hanelt, S.4    Schneider-Poetsch, H.A.5
  • 29
    • 0029818880 scopus 로고    scopus 로고
    • Similarity of a chromatic adaptation sensor to phytochrome and ethylene receptors
    • Kehoe D.M., Grossman A.R. Similarity of a chromatic adaptation sensor to phytochrome and ethylene receptors. Science 1996, 273:1409-1412.
    • (1996) Science , vol.273 , pp. 1409-1412
    • Kehoe, D.M.1    Grossman, A.R.2
  • 30
    • 0030912553 scopus 로고    scopus 로고
    • New classes of mutants in complementary chromatic adaptation provide evidence for a novel four-step phosphorelay system
    • Kehoe D.M., Grossman A.R. New classes of mutants in complementary chromatic adaptation provide evidence for a novel four-step phosphorelay system. J. Bacteriol. 1997, 179:3914-3921.
    • (1997) J. Bacteriol. , vol.179 , pp. 3914-3921
    • Kehoe, D.M.1    Grossman, A.R.2
  • 31
    • 0030940302 scopus 로고    scopus 로고
    • Disruption of a Synechocystis sp. PCC 6803 gene with partial similarity to phytochrome genes alters growth under changing light qualities
    • Wilde A., Churin Y., Schubert H., Borner T. Disruption of a Synechocystis sp. PCC 6803 gene with partial similarity to phytochrome genes alters growth under changing light qualities. FEBS Lett. 1997, 406:89-92.
    • (1997) FEBS Lett. , vol.406 , pp. 89-92
    • Wilde, A.1    Churin, Y.2    Schubert, H.3    Borner, T.4
  • 32
    • 0030865349 scopus 로고    scopus 로고
    • A Cyanobacterial phytochrome two-component light sensory system
    • Yeh K.C., Wu S.H., Murphy J.T., Lagarias J.C. A Cyanobacterial phytochrome two-component light sensory system. Science 1997, 277:1505-1508.
    • (1997) Science , vol.277 , pp. 1505-1508
    • Yeh, K.C.1    Wu, S.H.2    Murphy, J.T.3    Lagarias, J.C.4
  • 34
    • 0034733024 scopus 로고    scopus 로고
    • Chromophore-apoprotein interactions in Synechocystis sp. PCC6803 phytochrome Cph1
    • Park C.M., Shim J.Y., Yang S.S., Kang J.G., Kim J.I., Luka Z., Song P.S. Chromophore-apoprotein interactions in Synechocystis sp. PCC6803 phytochrome Cph1. Biochemistry 2000, 39:6349-6356.
    • (2000) Biochemistry , vol.39 , pp. 6349-6356
    • Park, C.M.1    Shim, J.Y.2    Yang, S.S.3    Kang, J.G.4    Kim, J.I.5    Luka, Z.6    Song, P.S.7
  • 36
    • 0034604449 scopus 로고    scopus 로고
    • CikA, a bacteriophytochrome that resets the cyanobacterial circadian clock
    • Schmitz O., Katayama M., Williams S.B., Kondo T., Golden S.S. CikA, a bacteriophytochrome that resets the cyanobacterial circadian clock. Science 2000, 289:765-768.
    • (2000) Science , vol.289 , pp. 765-768
    • Schmitz, O.1    Katayama, M.2    Williams, S.B.3    Kondo, T.4    Golden, S.S.5
  • 37
    • 0035912777 scopus 로고    scopus 로고
    • Light regulation of type IV pilus-dependent motility by chemosenor-like elements in Synechocystis PCC6803
    • Bhaya D., Takahashi A., Grossman A.R. Light regulation of type IV pilus-dependent motility by chemosenor-like elements in Synechocystis PCC6803. Proc. Natl. Acad. Sci. USA 2001, 98:7540-7545.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7540-7545
    • Bhaya, D.1    Takahashi, A.2    Grossman, A.R.3
  • 38
    • 0033575370 scopus 로고    scopus 로고
    • Bacterial photoreceptor with similarity to photoactive yellow protein and plant phytochromes
    • Jiang Z., Swem L.R., Rushing B.G., Devanathan S., Tollin G., Bauer C.E. Bacterial photoreceptor with similarity to photoactive yellow protein and plant phytochromes. Science 1999, 285:406-409.
    • (1999) Science , vol.285 , pp. 406-409
    • Jiang, Z.1    Swem, L.R.2    Rushing, B.G.3    Devanathan, S.4    Tollin, G.5    Bauer, C.E.6
  • 39
    • 0034494048 scopus 로고    scopus 로고
    • Bacteriophytochromes: New tools for understanding phytochrome signal transduction
    • Vierstra R.D., Davis S.J. Bacteriophytochromes: New tools for understanding phytochrome signal transduction. Sem. Cell. Dev. Biol. 2000, 11:511-521.
    • (2000) Sem. Cell. Dev. Biol. , vol.11 , pp. 511-521
    • Vierstra, R.D.1    Davis, S.J.2
  • 40
    • 0035856979 scopus 로고    scopus 로고
    • Bacteriophytochromes are photochromic histidine kinases that use a biliverdin chromophore
    • Bhoo S.-H., Davis S.J., Walker J.M., Karniol B., Vierstra R.D. Bacteriophytochromes are photochromic histidine kinases that use a biliverdin chromophore. Nature 2001, 414:776-779.
    • (2001) Nature , vol.414 , pp. 776-779
    • Bhoo, S.-H.1    Davis, S.J.2    Walker, J.M.3    Karniol, B.4    Vierstra, R.D.5
  • 41
    • 0033601199 scopus 로고    scopus 로고
    • Bacteriophytochromes: Phytochromelike photoreceptors from nonphotosynthetic eubacteria
    • Davis S.J., Vener A.V., Vierstra R.D. Bacteriophytochromes: Phytochromelike photoreceptors from nonphotosynthetic eubacteria. Science 1999, 286:2517-2520.
    • (1999) Science , vol.286 , pp. 2517-2520
    • Davis, S.J.1    Vener, A.V.2    Vierstra, R.D.3
  • 43
    • 0031989125 scopus 로고    scopus 로고
    • Fluorescence and photochemistry of recombinant phytochrome from the cyanobacterium Synechocystis
    • Sineshchekov V., Hughes J., Hartmann E., Lamparter T. Fluorescence and photochemistry of recombinant phytochrome from the cyanobacterium Synechocystis. Photochem. Photobiol. 1998, 67:263-267.
    • (1998) Photochem. Photobiol. , vol.67 , pp. 263-267
    • Sineshchekov, V.1    Hughes, J.2    Hartmann, E.3    Lamparter, T.4
  • 45
    • 0033397947 scopus 로고    scopus 로고
    • Prokaryotes and phytochrome. The connection to chromophores and signaling
    • Hughes J., Lamparter T. Prokaryotes and phytochrome. The connection to chromophores and signaling. Plant Physiol. 1999, 121:1059-1068.
    • (1999) Plant Physiol. , vol.121 , pp. 1059-1068
    • Hughes, J.1    Lamparter, T.2
  • 46
    • 9844254664 scopus 로고
    • Biosynthesis of phycobilins
    • Beale S.I. Biosynthesis of phycobilins. Chem. Rev. 1993, 93:785-802.
    • (1993) Chem. Rev. , vol.93 , pp. 785-802
    • Beale, S.I.1
  • 47
    • 0034857464 scopus 로고    scopus 로고
    • Characterization of the Cph1 holo-protein from Synechocystis sp. PCC6803
    • Hübschmann T., Börner T., Hartmann E., Lampartner T. Characterization of the Cph1 holo-protein from Synechocystis sp. PCC6803. Eur J. Biochem. 2001, 268:2005-2063.
    • (2001) Eur J. Biochem. , vol.268 , pp. 2005-2063
    • Hübschmann, T.1    Börner, T.2    Hartmann, E.3    Lampartner, T.4
  • 50
    • 0033612143 scopus 로고    scopus 로고
    • PKS1, a substrate phosphorylated by phytochrome that modulates light signaling in Arabidopsis
    • Fankhauser C., Yeh K.C., Lagarias J.C., Zhang H., Elich T.D., Chory J. PKS1, a substrate phosphorylated by phytochrome that modulates light signaling in Arabidopsis. Science 1999, 284:1539-1541.
    • (1999) Science , vol.284 , pp. 1539-1541
    • Fankhauser, C.1    Yeh, K.C.2    Lagarias, J.C.3    Zhang, H.4    Elich, T.D.5    Chory, J.6
  • 52
    • 0033545992 scopus 로고    scopus 로고
    • Poc1: An Arabidopsis mutant perturbed in phytochrome signaling because of a T-DNA insertion in the promoter of PIF3, a gene encoding a phytochrome-interacting BHLH protein
    • Halliday K.J., Hudson M., Ni M., Qin M., Quail P.H. poc1: An Arabidopsis mutant perturbed in phytochrome signaling because of a T-DNA insertion in the promoter of PIF3, a gene encoding a phytochrome-interacting BHLH protein. Proc. Natl. Acad. Sci. USA 1999, 96:5832-5837.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 5832-5837
    • Halliday, K.J.1    Hudson, M.2    Ni, M.3    Qin, M.4    Quail, P.H.5
  • 53
    • 0032567039 scopus 로고    scopus 로고
    • PIF3, a Phytochrome-interacting factor necessary for normal photoinduced signal transduction, is a novel basic helix-loop-helix protein
    • Ni M., Tepperman J.M., Quail P.H. PIF3, a Phytochrome-interacting factor necessary for normal photoinduced signal transduction, is a novel basic helix-loop-helix protein. Cell 1998, 95:657-667.
    • (1998) Cell , vol.95 , pp. 657-667
    • Ni, M.1    Tepperman, J.M.2    Quail, P.H.3
  • 54
    • 0033584359 scopus 로고    scopus 로고
    • Binding of phytochrome B to its nuclear sSignaling partner PIF3 is reversibly induced by light
    • Ni M., Tepperman J.M., Quail P.H. Binding of phytochrome B to its nuclear sSignaling partner PIF3 is reversibly induced by light. Nature 1999, 400:781-784.
    • (1999) Nature , vol.400 , pp. 781-784
    • Ni, M.1    Tepperman, J.M.2    Quail, P.H.3
  • 55
    • 0041029474 scopus 로고    scopus 로고
    • Direct targeting of light signals to a promoter element-bound transcription factor
    • Martinez-Garcia J.F., Huq E., Quail P.H. Direct targeting of light signals to a promoter element-bound transcription factor. Science 2000, 288:859-863.
    • (2000) Science , vol.288 , pp. 859-863
    • Martinez-Garcia, J.F.1    Huq, E.2    Quail, P.H.3
  • 56
    • 0032724828 scopus 로고    scopus 로고
    • Light quality-dependent nuclear import of the plant photoreceptors phytochrome A and B
    • Kircher S., Kozma-Bognar L., Kim L., Adam E., Harter K., Schafer E., Nagy F. Light quality-dependent nuclear import of the plant photoreceptors phytochrome A and B. Plant Cell 1999, 11:1445-1456.
    • (1999) Plant Cell , vol.11 , pp. 1445-1456
    • Kircher, S.1    Kozma-Bognar, L.2    Kim, L.3    Adam, E.4    Harter, K.5    Schafer, E.6    Nagy, F.7
  • 57
    • 0033869340 scopus 로고    scopus 로고
    • Light-Induced nuclear translocation of endogenous Pea phytochrome A visualized by immunocytochemical procedures
    • Hisada A., Hanzawa H., Weller J.L., Nagatani A., Reid J.B., Furuya M. Light-Induced nuclear translocation of endogenous Pea phytochrome A visualized by immunocytochemical procedures. Plant Cell. 2000, 12:1063-1078.
    • (2000) Plant Cell. , vol.12 , pp. 1063-1078
    • Hisada, A.1    Hanzawa, H.2    Weller, J.L.3    Nagatani, A.4    Reid, J.B.5    Furuya, M.6
  • 58
    • 0028332848 scopus 로고
    • Transduction mechanisms of vertebrate and invertebrate photoreceptors
    • Yarfitz S., Hurley J.B. Transduction mechanisms of vertebrate and invertebrate photoreceptors. J. Biol. Chem. 1994, 269:14329-14332.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14329-14332
    • Yarfitz, S.1    Hurley, J.B.2
  • 59
    • 0031251804 scopus 로고    scopus 로고
    • Characterization of regions within the N-terminal 6-kilodalton domain of phytochrome A that modulate its biological activity
    • Jordan E.T., Marita J.M., Clough R.C., Vierstra R.D. Characterization of regions within the N-terminal 6-kilodalton domain of phytochrome A that modulate its biological activity. Plant Physiol. 1997, 115:693-704.
    • (1997) Plant Physiol. , vol.115 , pp. 693-704
    • Jordan, E.T.1    Marita, J.M.2    Clough, R.C.3    Vierstra, R.D.4
  • 60
    • 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. Serine-to-alanine substitutions at the amino-terminal region of phytochrome A result in an increase in biological activity. Genes Dev. 1992, 6:2364-2372.
    • (1992) Genes Dev. , vol.6 , pp. 2364-2372
    • Stockhaus, J.1    Nagatani, A.2    Halfter, U.3    Kay, S.4    Furuya, M.5    Chua, N.H.6
  • 61
    • 0033041152 scopus 로고    scopus 로고
    • Sequences within both the N- and C-terminal domains of phytochrome A are required for Pfr ubiquitination and degradation
    • Clough R.C., Jordan-Beebe E.T., Lohman K.N., Marita J.M., Walker J.M., Gatz C., Vierstra R.D. Sequences within both the N- and C-terminal domains of phytochrome A are required for Pfr ubiquitination and degradation. Plant J. 1999, 17:155-167.
    • (1999) Plant J. , vol.17 , pp. 155-167
    • Clough, R.C.1    Jordan-Beebe, E.T.2    Lohman, K.N.3    Marita, J.M.4    Walker, J.M.5    Gatz, C.6    Vierstra, R.D.7
  • 62
    • 0030267548 scopus 로고    scopus 로고
    • Proteolysis in Plants: Mechanisms and functions
    • Vierstra R.D. Proteolysis in Plants: Mechanisms and functions. Plant Mol. Biol. 1996, 32:275-302.
    • (1996) Plant Mol. Biol. , vol.32 , pp. 275-302
    • Vierstra, R.D.1
  • 64
    • 0001284908 scopus 로고
    • Purification and initial characterization of 124-kilodalton phytochrome from Avena
    • Vierstra R.D., Quail P.H. Purification and initial characterization of 124-kilodalton phytochrome from Avena. Biochemistry 1983, 22:2498-2505.
    • (1983) Biochemistry , vol.22 , pp. 2498-2505
    • Vierstra, R.D.1    Quail, P.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.