메뉴 건너뛰기




Volumn 281, Issue 9, 2014, Pages 2299-2311

A novel cryptochrome in the diatom Phaeodactylum tricornutum influences the regulation of light-harvesting protein levels

Author keywords

5,10 methenyltetrahydrofolate (MTHF); algae; FAD; Lhcf; Lhcx

Indexed keywords

5,10 METHENYLTETRAHYDROFOLATE; CRYPTOCHROME; CYCLOBUTANE; CYCLOBUTANE PYRIMIDINE DIMER PHOTOLYASE; DASH CRYPTOCHROME; DIMER; LYASE; MICROORGANISM PROTEIN; PROTEIN CRYP; PROTEIN LHCF; PROTEIN LHCX; PYRIMIDINE; TETRAHYDROFOLIC ACID; UNCLASSIFIED DRUG;

EID: 84899911009     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12782     Document Type: Article
Times cited : (55)

References (67)
  • 2
    • 33750713440 scopus 로고    scopus 로고
    • A cryptochrome/photolyase class of enzymes with single-stranded DNA-specific photolyase activity
    • Selby CP, &, Sancar A, (2006) A cryptochrome/photolyase class of enzymes with single-stranded DNA-specific photolyase activity. Proc Natl Acad Sci USA 103, 17696-17700.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 17696-17700
    • Selby, C.P.1    Sancar, A.2
  • 3
    • 58549111388 scopus 로고    scopus 로고
    • Recognition and repair of UV lesions in loop structures of duplex DNA by DASH-type cryptochrome
    • Pokorny R, Klar T, Hennecke U, Carell T, Batschauer A, &, Essen L, (2008) Recognition and repair of UV lesions in loop structures of duplex DNA by DASH-type cryptochrome. Proc Natl Acad Sci USA 105, 21023-21027.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 21023-21027
    • Pokorny, R.1    Klar, T.2    Hennecke, U.3    Carell, T.4    Batschauer, A.5    Essen, L.6
  • 5
    • 0027493250 scopus 로고
    • HY4 gene of A. Thaliana encodes a protein with characteristics of a blue-light photoreceptor
    • Ahmad M, &, Cashmore AR, (1993) HY4 gene of A. thaliana encodes a protein with characteristics of a blue-light photoreceptor. Nature 366, 162-166.
    • (1993) Nature , vol.366 , pp. 162-166
    • Ahmad, M.1    Cashmore, A.R.2
  • 6
    • 0038305458 scopus 로고    scopus 로고
    • Structure and function of DNA photolyase and cryptochrome blue-light photoreceptors
    • Sancar A, (2003) Structure and function of DNA photolyase and cryptochrome blue-light photoreceptors. Chem Rev 103, 2203-2238.
    • (2003) Chem Rev , vol.103 , pp. 2203-2238
    • Sancar, A.1
  • 7
    • 33748461650 scopus 로고    scopus 로고
    • Absorption and fluorescence spectroscopic characterization of cryptochrome 3 from Arabidopsis thaliana
    • Song S, Dick B, Penzkofer A, Pokorny R, Batschauer A, &, Essen L, (2006) Absorption and fluorescence spectroscopic characterization of cryptochrome 3 from Arabidopsis thaliana. J Photochem Photobiol B 85, 1-16.
    • (2006) J Photochem Photobiol B , vol.85 , pp. 1-16
    • Song, S.1    Dick, B.2    Penzkofer, A.3    Pokorny, R.4    Batschauer, A.5    Essen, L.6
  • 9
    • 37749026998 scopus 로고    scopus 로고
    • The fluorescence yield of the trimeric fucoxanthin-chlorophyll-protein FCPa in the diatom Cyclotella meneghiniana is dependent on the amount of bound diatoxanthin
    • Gundermann K, &, Büchel C, (2008) The fluorescence yield of the trimeric fucoxanthin-chlorophyll-protein FCPa in the diatom Cyclotella meneghiniana is dependent on the amount of bound diatoxanthin. Photosynth Res 95, 229-235.
    • (2008) Photosynth Res , vol.95 , pp. 229-235
    • Gundermann, K.1    Büchel, C.2
  • 10
    • 84860998877 scopus 로고    scopus 로고
    • Factors determining the fluorescence yield of fucoxanthin-chlorophyll complexes (FCP) involved in non-photochemical quenching in diatoms
    • Gundermann K, &, Büchel C, (2012) Factors determining the fluorescence yield of fucoxanthin-chlorophyll complexes (FCP) involved in non-photochemical quenching in diatoms. Biochim Biophys Acta 1817, 1044-1052.
    • (2012) Biochim Biophys Acta , vol.1817 , pp. 1044-1052
    • Gundermann, K.1    Büchel, C.2
  • 11
    • 77957301015 scopus 로고    scopus 로고
    • Effects of iron and copper deficiency on the expression of members of the light-harvesting family in the diatom Thalassiosira pseudonana (Bacillariophyceae)
    • Zhu S, Guo J, Maldonado MT, &, Green BR, (2010) Effects of iron and copper deficiency on the expression of members of the light-harvesting family in the diatom Thalassiosira pseudonana (Bacillariophyceae). J Phycol 46, 974-981.
    • (2010) J Phycol , vol.46 , pp. 974-981
    • Zhu, S.1    Guo, J.2    Maldonado, M.T.3    Green, B.R.4
  • 14
    • 84857934015 scopus 로고    scopus 로고
    • Exploring the molecular basis of responses to light in marine diatoms
    • Depauw FA, Rogato A, Ribera d'Alcalá M, &, Falciatore A, (2012) Exploring the molecular basis of responses to light in marine diatoms. J Exp Bot 63, 1575-1591.
    • (2012) J Exp Bot , vol.63 , pp. 1575-1591
    • Depauw, F.A.1    Rogato, A.2    Ribera D'Alcalá, M.3    Falciatore, A.4
  • 15
    • 0028559513 scopus 로고
    • A new class of DNA photolyases present in various organisms including aplacental mammals
    • Yasui A, Eker AP, Yasuhira S, Yajima H, Kobayashi T, Takao M, &, Oikawa A, (1994) A new class of DNA photolyases present in various organisms including aplacental mammals. EMBO J 13, 6143-6151.
    • (1994) EMBO J , vol.13 , pp. 6143-6151
    • Yasui, A.1    Eker, A.P.2    Yasuhira, S.3    Yajima, H.4    Kobayashi, T.5    Takao, M.6    Oikawa, A.7
  • 18
    • 84876924958 scopus 로고    scopus 로고
    • Crystal structure of a prokaryotic (6-4) photolyase with an Fe-S cluster and a 6,7-dimethyl-8-ribityllumazine antenna chromophore
    • Zhang F, Scheerer P, Oberpichler I, Lamparter T, &, Krauss N, (2013) Crystal structure of a prokaryotic (6-4) photolyase with an Fe-S cluster and a 6,7-dimethyl-8-ribityllumazine antenna chromophore. Proc Natl Acad Sci USA 110, 7217-7222.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 7217-7222
    • Zhang, F.1    Scheerer, P.2    Oberpichler, I.3    Lamparter, T.4    Krauss, N.5
  • 19
    • 84857792144 scopus 로고    scopus 로고
    • CryB from Rhodobacter sphaeroides: A unique class of cryptochromes with new cofactors
    • Geisselbrecht Y, Frühwirth S, Schroeder C, Pierik AJ, Klug G, &, Essen L, (2012) CryB from Rhodobacter sphaeroides: a unique class of cryptochromes with new cofactors. EMBO Rep 13, 223-229.
    • (2012) EMBO Rep , vol.13 , pp. 223-229
    • Geisselbrecht, Y.1    Frühwirth, S.2    Schroeder, C.3    Pierik, A.J.4    Klug, G.5    Essen, L.6
  • 20
    • 0013954466 scopus 로고
    • On the existence of spectrally distinct classes of flavoprotein semiquinones. A new method for the quantitative production of flavoprotein semiquinones
    • Massey V, &, Palmer G, (1966) On the existence of spectrally distinct classes of flavoprotein semiquinones. A new method for the quantitative production of flavoprotein semiquinones. Biochemistry 5, 3181-3189.
    • (1966) Biochemistry , vol.5 , pp. 3181-3189
    • Massey, V.1    Palmer, G.2
  • 21
    • 0018067152 scopus 로고
    • Quantitative determination of noncovalently bound flavins: Types and methods of analysis
    • Siegel LM, (1978) Quantitative determination of noncovalently bound flavins: types and methods of analysis. Methods Enzymol 53, 419-429.
    • (1978) Methods Enzymol , vol.53 , pp. 419-429
    • Siegel, L.M.1
  • 22
    • 0025100995 scopus 로고
    • Chromophore function and interaction in Escherichia coli DNA photolyase: Reconstitution of the apoenzyme with pterin and/or flavin derivatives
    • Jorns MS, Wang BY, Jordan SP, &, Chanderkar LP, (1990) Chromophore function and interaction in Escherichia coli DNA photolyase: reconstitution of the apoenzyme with pterin and/or flavin derivatives. Biochemistry 29, 552-561.
    • (1990) Biochemistry , vol.29 , pp. 552-561
    • Jorns, M.S.1    Wang, B.Y.2    Jordan, S.P.3    Chanderkar, L.P.4
  • 23
    • 67449128223 scopus 로고    scopus 로고
    • Fluorescence behaviour of 5,10-methenyltetrahydrofolate, 10-formyltetrahydrofolate, 10-formyldihydrofolate, and 10-formylfolate in aqueous solution at pH 8
    • Tyagi A, Penzkofer A, Batschauer A, &, Wolf E, (2009) Fluorescence behaviour of 5,10-methenyltetrahydrofolate, 10-formyltetrahydrofolate, 10-formyldihydrofolate, and 10-formylfolate in aqueous solution at pH 8. Chem Phys 361, 75-82.
    • (2009) Chem Phys , vol.361 , pp. 75-82
    • Tyagi, A.1    Penzkofer, A.2    Batschauer, A.3    Wolf, E.4
  • 26
    • 84871966213 scopus 로고    scopus 로고
    • Identification of several sub-populations in the pool of light harvesting proteins in the pennate diatom Phaeodactylum tricornutum
    • Gundermann K, Schmidt M, Weisheit W, Mittag M, &, Büchel C, (2013) Identification of several sub-populations in the pool of light harvesting proteins in the pennate diatom Phaeodactylum tricornutum. Biochim Biophys Acta 1827, 303-310.
    • (2013) Biochim Biophys Acta , vol.1827 , pp. 303-310
    • Gundermann, K.1    Schmidt, M.2    Weisheit, W.3    Mittag, M.4    Büchel, C.5
  • 27
    • 77956444369 scopus 로고    scopus 로고
    • Characterization of two members of the cryptochrome/photolyase family from Ostreococcus tauri provides insights into the origin and evolution of cryptochromes
    • Heijde M, Zabulon G, Corellou F, Ishikawa T, Brazard J, Usman A, Sanchez F, Plaza P, Martin M, Falciatore A, et al,. (2010) Characterization of two members of the cryptochrome/photolyase family from Ostreococcus tauri provides insights into the origin and evolution of cryptochromes. Plant Cell Environ 33, 1614-1626.
    • (2010) Plant Cell Environ , vol.33 , pp. 1614-1626
    • Heijde, M.1    Zabulon, G.2    Corellou, F.3    Ishikawa, T.4    Brazard, J.5    Usman, A.6    Sanchez, F.7    Plaza, P.8    Martin, M.9    Falciatore, A.10
  • 29
    • 84859544483 scopus 로고    scopus 로고
    • Photoantenna in two cryptochrome-photolyase proteins from O. Tauri: Presence, nature and ultrafast photoinduced dynamics
    • Brazard J, Ley C, Lacombat F, Plaza P, Mony L, Heijde M, Zabulon G, &, Bowler C, (2012) Photoantenna in two cryptochrome-photolyase proteins from O. tauri: presence, nature and ultrafast photoinduced dynamics. J Photochem Photobiol A 234, 135-145.
    • (2012) J Photochem Photobiol A , vol.234 , pp. 135-145
    • Brazard, J.1    Ley, C.2    Lacombat, F.3    Plaza, P.4    Mony, L.5    Heijde, M.6    Zabulon, G.7    Bowler, C.8
  • 30
    • 20444366979 scopus 로고    scopus 로고
    • Ultrafast dynamics of resonance energy transfer in cryptochrome
    • Saxena C, Wang H, Kavakli IH, Sancar A, &, Zhong D, (2005) Ultrafast dynamics of resonance energy transfer in cryptochrome. J Am Chem Soc 127, 7984-7985.
    • (2005) J Am Chem Soc , vol.127 , pp. 7984-7985
    • Saxena, C.1    Wang, H.2    Kavakli, I.H.3    Sancar, A.4    Zhong, D.5
  • 33
    • 48349113795 scopus 로고    scopus 로고
    • Evidence of a light-sensing role for folate in Arabidopsis cryptochrome blue-light receptors
    • Hoang N, Bouly J, &, Ahmad M, (2008) Evidence of a light-sensing role for folate in Arabidopsis cryptochrome blue-light receptors. Mol Plant 1, 68-74.
    • (2008) Mol Plant , vol.1 , pp. 68-74
    • Hoang, N.1    Bouly, J.2    Ahmad, M.3
  • 34
    • 34547592093 scopus 로고    scopus 로고
    • Blue light induces radical formation and autophosphorylation in the light-sensitive domain of Chlamydomonas cryptochrome
    • Immeln D, Schlesinger R, Heberle J, &, Kottke T, (2007) Blue light induces radical formation and autophosphorylation in the light-sensitive domain of Chlamydomonas cryptochrome. J Biol Chem 282, 21720-21728.
    • (2007) J Biol Chem , vol.282 , pp. 21720-21728
    • Immeln, D.1    Schlesinger, R.2    Heberle, J.3    Kottke, T.4
  • 35
    • 79953743213 scopus 로고    scopus 로고
    • Photoreaction of plant and DASH cryptochromes probed by infrared spectroscopy: The neutral radical state of flavoproteins
    • Immeln D, Pokorny R, Herman E, Moldt J, Batschauer A, &, Kottke T, (2010) Photoreaction of plant and DASH cryptochromes probed by infrared spectroscopy: the neutral radical state of flavoproteins. J Phys Chem B 114, 17155-17161.
    • (2010) J Phys Chem B , vol.114 , pp. 17155-17161
    • Immeln, D.1    Pokorny, R.2    Herman, E.3    Moldt, J.4    Batschauer, A.5    Kottke, T.6
  • 36
    • 84255201401 scopus 로고    scopus 로고
    • Direkte Detektion eines lichtinduzierten Radikalpaars in einem Cryptochrom-Blaulichtrezeptor
    • Biskup T, Schleicher E, Okafuji A, Link G, Hitomi K, Getzoff ED, &, Weber S, (2009) Direkte Detektion eines lichtinduzierten Radikalpaars in einem Cryptochrom-Blaulichtrezeptor. Angew Chem 121, 411-415.
    • (2009) Angew Chem , vol.121 , pp. 411-415
    • Biskup, T.1    Schleicher, E.2    Okafuji, A.3    Link, G.4    Hitomi, K.5    Getzoff, E.D.6    Weber, S.7
  • 39
    • 52149085899 scopus 로고    scopus 로고
    • Involvement of electron transfer in the photoreaction of zebrafish cryptochrome-DASH
    • Zikihara K, Ishikawa T, Todo T, &, Tokutomi S, (2008) Involvement of electron transfer in the photoreaction of zebrafish cryptochrome-DASH. Photochem Photobiol 84, 1016-1023.
    • (2008) Photochem Photobiol , vol.84 , pp. 1016-1023
    • Zikihara, K.1    Ishikawa, T.2    Todo, T.3    Tokutomi, S.4
  • 40
    • 73149114186 scopus 로고    scopus 로고
    • Kinetic stability of the flavin semiquinone in photolyase and cryptochrome-DASH
    • Damiani MJ, Yalloway GN, Lu J, McLeod NR, &, O'Neill MA, (2009) Kinetic stability of the flavin semiquinone in photolyase and cryptochrome-DASH. Biochemistry 48, 11399-11411.
    • (2009) Biochemistry , vol.48 , pp. 11399-11411
    • Damiani, M.J.1    Yalloway, G.N.2    Lu, J.3    McLeod, N.R.4    O'Neill, M.A.5
  • 41
    • 33644553813 scopus 로고    scopus 로고
    • Blue-light-induced changes in Arabidopsis cryptochrome 1 probed by FTIR difference spectroscopy
    • Kottke T, Batschauer A, Ahmad M, &, Heberle J, (2006) Blue-light-induced changes in Arabidopsis cryptochrome 1 probed by FTIR difference spectroscopy. Biochemistry 45, 2472-2479.
    • (2006) Biochemistry , vol.45 , pp. 2472-2479
    • Kottke, T.1    Batschauer, A.2    Ahmad, M.3    Heberle, J.4
  • 42
    • 27744589610 scopus 로고    scopus 로고
    • Identification and characterization of a second chromophore of DNA photolyase from Thermus thermophilus HB27
    • Ueda T, Kato A, Kuramitsu S, Terasawa H, &, Shimada I, (2005) Identification and characterization of a second chromophore of DNA photolyase from Thermus thermophilus HB27. J Biol Chem 280, 36237-36243.
    • (2005) J Biol Chem , vol.280 , pp. 36237-36243
    • Ueda, T.1    Kato, A.2    Kuramitsu, S.3    Terasawa, H.4    Shimada, I.5
  • 43
    • 0033545878 scopus 로고    scopus 로고
    • Intraprotein electron transfer between tyrosine and tryptophan in DNA photolyase from Anacystis nidulans
    • Aubert C, Mathis P, Eker APM, &, Brettel K, (1999) Intraprotein electron transfer between tyrosine and tryptophan in DNA photolyase from Anacystis nidulans. Proc Natl Acad Sci USA 96, 5423-5427.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 5423-5427
    • Aubert, C.1    Mathis, P.2    Eker, A.P.M.3    Brettel, K.4
  • 45
    • 84874765332 scopus 로고    scopus 로고
    • Molecular and photosynthetic responses to prolonged darkness and subsequent acclimation to re-illumination in the diatom Phaeodactylum tricornutum
    • Nymark M, Valle KC, Hancke K, Winge P, Andresen K, Johnsen G, Bones AM, Brembu T, &, Subramanyam R, (2013) Molecular and photosynthetic responses to prolonged darkness and subsequent acclimation to re-illumination in the diatom Phaeodactylum tricornutum. PLoS One 8, e58722.
    • (2013) PLoS One , vol.8
    • Nymark, M.1    Valle, K.C.2    Hancke, K.3    Winge, P.4    Andresen, K.5    Johnsen, G.6    Bones, A.M.7    Brembu, T.8    Subramanyam, R.9
  • 46
    • 34249039514 scopus 로고    scopus 로고
    • Characterization of a dinoflagellate cryptochrome blue-light receptor with a possible role in circadian control of the cell cycle
    • Brunelle SA, Hazard ES, Sotka EE, &, van Dolah FM, (2007) Characterization of a dinoflagellate cryptochrome blue-light receptor with a possible role in circadian control of the cell cycle. J Phycol 43, 509-518.
    • (2007) J Phycol , vol.43 , pp. 509-518
    • Brunelle, S.A.1    Hazard, E.S.2    Sotka, E.E.3    Van Dolah, F.M.4
  • 47
    • 0032916354 scopus 로고    scopus 로고
    • Circadian expression of the light-harvesting complex protein genes in plants
    • Piechulla B, (1999) Circadian expression of the light-harvesting complex protein genes in plants. Chronobiol Int 16, 115-128.
    • (1999) Chronobiol Int , vol.16 , pp. 115-128
    • Piechulla, B.1
  • 48
    • 78649798968 scopus 로고    scopus 로고
    • Evidence for the existence of one antenna-associated lipid-dissolved and two protein-bound pools of diadinoxanthin cycle pigments in diatoms
    • Lepetit B, Volke D, Gilbert M, Wilhelm C, &, Goss R, (2010) Evidence for the existence of one antenna-associated lipid-dissolved and two protein-bound pools of diadinoxanthin cycle pigments in diatoms. Plant Physiol 154, 1905-1920.
    • (2010) Plant Physiol , vol.154 , pp. 1905-1920
    • Lepetit, B.1    Volke, D.2    Gilbert, M.3    Wilhelm, C.4    Goss, R.5
  • 49
    • 82755182012 scopus 로고    scopus 로고
    • The thylakoid membrane proteome of two marine diatoms outlines both diatom-specific and species-specific features of the photosynthetic machinery
    • Grouneva I, Rokka A, &, Aro E, (2011) The thylakoid membrane proteome of two marine diatoms outlines both diatom-specific and species-specific features of the photosynthetic machinery. J Proteome Res 10, 5338-5353.
    • (2011) J Proteome Res , vol.10 , pp. 5338-5353
    • Grouneva, I.1    Rokka, A.2    Aro, E.3
  • 50
    • 34548286317 scopus 로고    scopus 로고
    • Spectroscopic and molecular characterization of the oligomeric antenna of the diatom Phaeodactylum tricornutum
    • Lepetit B, Volke D, Szabõ M, Hoffmann R, Garab G, Wilhelm C, &, Goss R, (2007) Spectroscopic and molecular characterization of the oligomeric antenna of the diatom Phaeodactylum tricornutum. Biochemistry 46, 9813-9822.
    • (2007) Biochemistry , vol.46 , pp. 9813-9822
    • Lepetit, B.1    Volke, D.2    Szabõ, M.3    Hoffmann, R.4    Garab, G.5    Wilhelm, C.6    Goss, R.7
  • 51
    • 0035294665 scopus 로고    scopus 로고
    • Changes in the photosynthetic apparatus of diatoms in response to low and high light intensities
    • Janssen M, Bathke L, Marquardt J, Krumbein WE, &, Rhiel E, (2001) Changes in the photosynthetic apparatus of diatoms in response to low and high light intensities. Int Microbiol 4, 27-33.
    • (2001) Int Microbiol , vol.4 , pp. 27-33
    • Janssen, M.1    Bathke, L.2    Marquardt, J.3    Krumbein, W.E.4    Rhiel, E.5
  • 52
    • 33646423824 scopus 로고    scopus 로고
    • Immuno-electron microscopic quantification of the fucoxanthin chlorophyll a/c binding polypeptides Fcp2, Fcp4, and Fcp6 of Cyclotella cryptica grown under low- and high-light intensities
    • Becker F, &, Rhiel E, (2006) Immuno-electron microscopic quantification of the fucoxanthin chlorophyll a/c binding polypeptides Fcp2, Fcp4, and Fcp6 of Cyclotella cryptica grown under low- and high-light intensities. Int Microbiol 9, 29-36.
    • (2006) Int Microbiol , vol.9 , pp. 29-36
    • Becker, F.1    Rhiel, E.2
  • 53
    • 33751082107 scopus 로고    scopus 로고
    • Subunit composition and pigmentation of fucoxanthin-chlorophyll proteins in diatoms: Evidence for a subunit involved in diadinoxanthin and diatoxanthin binding
    • Beer A, Gundermann K, Beckmann J, &, Büchel C, (2006) Subunit composition and pigmentation of fucoxanthin-chlorophyll proteins in diatoms: evidence for a subunit involved in diadinoxanthin and diatoxanthin binding. Biochemistry 45, 13046-13053.
    • (2006) Biochemistry , vol.45 , pp. 13046-13053
    • Beer, A.1    Gundermann, K.2    Beckmann, J.3    Büchel, C.4
  • 54
    • 84872278861 scopus 로고    scopus 로고
    • Blue light is essential for high light acclimation and photoprotection in the diatom Phaeodactylum tricornutum
    • Schellenberger Costa B, Jungandreas A, Jakob T, Weisheit W, Mittag M, &, Wilhelm C, (2013) Blue light is essential for high light acclimation and photoprotection in the diatom Phaeodactylum tricornutum. J Exp Bot 64, 483-493.
    • (2013) J Exp Bot , vol.64 , pp. 483-493
    • Schellenberger Costa, B.1    Jungandreas, A.2    Jakob, T.3    Weisheit, W.4    Mittag, M.5    Wilhelm, C.6
  • 57
    • 84877349109 scopus 로고    scopus 로고
    • Blue-light-induced unfolding of the Jα helix allows for the dimerization of aureochrome-LOV from the diatom Phaeodactylum tricornutum
    • Herman E, Sachse M, Kroth PG, &, Kottke T, (2013) Blue-light-induced unfolding of the Jα helix allows for the dimerization of aureochrome-LOV from the diatom Phaeodactylum tricornutum. Biochemistry 52, 3094-3101.
    • (2013) Biochemistry , vol.52 , pp. 3094-3101
    • Herman, E.1    Sachse, M.2    Kroth, P.G.3    Kottke, T.4
  • 59
    • 19044369033 scopus 로고    scopus 로고
    • The circadian clock in Chlamydomonas reinhardtii. What is it for? What is it similar to?
    • Mittag M, Kiaulehn S, &, Johnson CH, (2005) The circadian clock in Chlamydomonas reinhardtii. What is it for? What is it similar to? Plant Physiol 137, 399-409.
    • (2005) Plant Physiol , vol.137 , pp. 399-409
    • Mittag, M.1    Kiaulehn, S.2    Johnson, C.H.3
  • 60
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular evolutionary genetics analysis (MEGA) software version 4.0
    • Tamura K, Dudley J, Nei M, &, Kumar S, (2007) MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol Biol Evol 24, 1596-1599.
    • (2007) Mol Biol Evol , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 61
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N, &, Nei M, (1987) The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 4, 406-425.
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 63
    • 0033855410 scopus 로고    scopus 로고
    • Transformation of the diatom Phaeodactylum tricornutum (Bacillariophyceae) with a variety of selectable marker and reporter genes
    • Zaslavskaia LA, Lippmeier JC, Kroth PG, Grossman AR, &, Apt KE, (2000) Transformation of the diatom Phaeodactylum tricornutum (Bacillariophyceae) with a variety of selectable marker and reporter genes. J Phycol 36, 379-386.
    • (2000) J Phycol , vol.36 , pp. 379-386
    • Zaslavskaia, L.A.1    Lippmeier, J.C.2    Kroth, P.G.3    Grossman, A.R.4    Apt, K.E.5
  • 64
    • 77956667519 scopus 로고    scopus 로고
    • Characterization of a trimeric light-harvesting complex in the diatom Phaeodactylum tricornutum built of FcpA and FcpE proteins
    • Joshi-Deo J, Schmidt M, Gruber A, Weisheit W, Mittag M, Kroth PG, &, Büchel C, (2010) Characterization of a trimeric light-harvesting complex in the diatom Phaeodactylum tricornutum built of FcpA and FcpE proteins. J Exp Bot 61, 3079-3087.
    • (2010) J Exp Bot , vol.61 , pp. 3079-3087
    • Joshi-Deo, J.1    Schmidt, M.2    Gruber, A.3    Weisheit, W.4    Mittag, M.5    Kroth, P.G.6    Büchel, C.7
  • 65
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger H, &, von Jagow G, (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166, 368-379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 66
    • 84863653613 scopus 로고    scopus 로고
    • Properties of photosystem i antenna protein complexes of the diatom Cyclotella meneghiniana
    • Juhas M, &, Büchel C, (2012) Properties of photosystem I antenna protein complexes of the diatom Cyclotella meneghiniana. J Exp Bot 63, 3673-3681.
    • (2012) J Exp Bot , vol.63 , pp. 3673-3681
    • Juhas, M.1    Büchel, C.2
  • 67
    • 26844582518 scopus 로고    scopus 로고
    • Localisation of fucoxanthin chlorophyll a/c-binding polypeptides of the centric diatom Cyclotella cryptica by immuno-electron microscopy
    • Westermann M, &, Rhiel E, (2005) Localisation of fucoxanthin chlorophyll a/c-binding polypeptides of the centric diatom Cyclotella cryptica by immuno-electron microscopy. Protoplasma 225, 217-223.
    • (2005) Protoplasma , vol.225 , pp. 217-223
    • Westermann, M.1    Rhiel, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.