메뉴 건너뛰기




Volumn 287, Issue 13, 2012, Pages 9901-9909

Mutations in N-terminal flanking region of blue light-sensing light-oxygen and voltage 2 (LOV2) domain disrupt its repressive activity on kinase domain in the Chlamydomonas phototropin

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELL PROLIFERATION; CHROMOPHORES; OXYGEN; YEAST;

EID: 84858952820     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.324723     Document Type: Article
Times cited : (48)

References (49)
  • 1
    • 34250183058 scopus 로고    scopus 로고
    • Phototropin blue light receptors
    • Christie, J. M. (2007) Phototropin blue light receptors. Annu. Rev. Plant Biol. 58, 21-45
    • (2007) Annu. Rev. Plant Biol. , vol.58 , pp. 21-45
    • Christie, J.M.1
  • 2
    • 0031470701 scopus 로고    scopus 로고
    • Arabidopsis NPH1: A protein kinase with a putative redox-sensing domain
    • DOI 10.1126/science.278.5346.2120
    • Huala, E., Oeller, P. W., Liscum, E., Han, I. S., Larsen, E., and Briggs, W. R. (1997) Arabidopsis NPH1: a protein kinase with a putative redox-sensing domain. Science 278, 2120-2123 (Pubitemid 28028321)
    • (1997) Science , vol.278 , Issue.5346 , pp. 2120-2123
    • Huala, E.1    Oeller, P.W.2    Liscum, E.3    Han, I.-S.4    Larsen, E.5    Briggs, W.R.6
  • 4
    • 0035912211 scopus 로고    scopus 로고
    • Phototropin-related NPL1 controls chloroplast relocation induced by blue light
    • DOI 10.1038/35073622
    • Jarillo, J. A., Gabrys, H., Capel, J., Alonso, J. M., Ecker, J. R., and Cashmore, A. R. (2001) Phototropin-related NPL1 controls chloroplast relocation induced by blue light. Nature 410, 952-954 (Pubitemid 32335843)
    • (2001) Nature , vol.410 , Issue.6831 , pp. 952-954
    • Jarillo, J.A.1    Gabrys, H.2    Capel, J.3    Alonso, J.M.4    Ecker, J.R.5    Cashmore, A.R.6
  • 5
    • 0035896393 scopus 로고    scopus 로고
    • Arabidopsis NPL1: A phototropin homolog controlling the chloroplast high-light avoidance response
    • DOI 10.1126/science.291.5511.2138
    • Kagawa, T., Sakai, T., Suetsugu, N., Oikawa, K., Ishiguro, S., Kato, T., Tabata, S., Okada, K., and Wada, M. (2001) Arabidopsis NPL1: a phototropin homolog controlling the chloroplast high-light avoidance response. Science 291, 2138-2141 (Pubitemid 32224442)
    • (2001) Science , vol.291 , Issue.5511 , pp. 2138-2141
    • Kagawa, T.1    Sakai, T.2    Suetsugu, N.3    Oikawa, K.4    Ishiguro, S.5    Kato, T.6    Tabata, S.7    Okada, K.8    Wada, M.9
  • 6
    • 0035818967 scopus 로고    scopus 로고
    • phot1 and phot2 mediate blue light regulation of stomatal opening
    • DOI 10.1038/414656a
    • Kinoshita, T., Doi, M., Suetsugu, N., Kagawa, T., Wada, M., and Shimazaki, K. (2001) Phot1 and phot2 mediate blue light regulation of stomatal opening. Nature 414, 656-660 (Pubitemid 33151263)
    • (2001) Nature , vol.414 , Issue.6864 , pp. 656-660
    • Kinoshita, T.1    Doi, M.2    Suetsugu, N.3    Kagawa, T.4    Wada, M.5    Shimazaki, K.-I.6
  • 7
    • 0036671887 scopus 로고    scopus 로고
    • Cellular and subcellular localization of phototropin 1
    • DOI 10.1105/tpc.003293
    • Sakamoto, K., and Briggs, W. R. (2002) Cellular and subcellular localization of phototropin 1. Plant Cell 14, 1723-1735 (Pubitemid 35002931)
    • (2002) Plant Cell , vol.14 , Issue.8 , pp. 1723-1735
    • Sakamoto, K.1    Briggs, W.R.2
  • 8
    • 82755166973 scopus 로고    scopus 로고
    • Tissue-autonomous promotion of palisade cell development by phototropin 2 in Arabidopsis
    • Kozuka, T., Kong, S. G., Doi, M., Shimazaki, K., and Nagatani, A. (2011) Tissue-autonomous promotion of palisade cell development by phototropin 2 in Arabidopsis. Plant Cell 23, 3684-3695
    • (2011) Plant Cell , vol.23 , pp. 3684-3695
    • Kozuka, T.1    Kong, S.G.2    Doi, M.3    Shimazaki, K.4    Nagatani, A.5
  • 9
    • 0037687415 scopus 로고    scopus 로고
    • Phototropin is the blue-light receptor that controls multiple steps in the sexual life cycle of the green alga Chlamydomonas reinhardtii
    • DOI 10.1073/pnas.0931459100
    • Huang, K., and Beck, C. F. (2003) Phototropin is the blue light receptor that controls multiple steps in the sexual life cycle of the green alga Chlamydomonas reinhardtii. Proc. Natl. Acad. Sci. U.S.A. 100, 6269-6274 (Pubitemid 36576965)
    • (2003) Proceedings of the National Academy of Sciences of the United States of America , vol.100 , Issue.10 , pp. 6269-6274
    • Huang, K.1    Beck, C.F.2
  • 10
    • 33745957287 scopus 로고    scopus 로고
    • Phototropin involvement in the expression of genes encoding chlorophyll and carotenoid biosynthesis enzymes and LHC apoproteins in Chlamydomonas reinhardtii
    • DOI 10.1111/j.1365-313X.2006.02852.x
    • Im, C. S., Eberhard, S., Huang, K., Beck, C. F., and Grossman, A. R. (2006) Phototropin involvement in the expression of genes encoding chlorophyll and carotenoid biosynthesis enzymes and LHC apoproteins in Chlamydomonas reinhardtii. Plant J. 48, 1-16 (Pubitemid 44379708)
    • (2006) Plant Journal , vol.48 , Issue.1 , pp. 1-16
    • Im, C.-S.1    Eberhard, S.2    Huang, K.3    Beck, C.F.4    Grossman, A.R.5
  • 12
    • 36549031157 scopus 로고    scopus 로고
    • Plant evolution: AGC kinases tell the auxin tale
    • DOI 10.1016/j.tplants.2007.10.004, PII S1360138507002750
    • Galván-Ampudia, C. S., and Offringa, R. (2007) Plant evolution: AGC kinases tell the auxin tale. Trends Plant Sci. 12, 541-547 (Pubitemid 350181562)
    • (2007) Trends in Plant Science , vol.12 , Issue.12 , pp. 541-547
    • Galvan-Ampudia, C.S.1    Offringa, R.2
  • 17
    • 34548118780 scopus 로고    scopus 로고
    • The C-terminal kinase fragment of Arabidopsis phototropin 2 triggers constitutive phototropin responses
    • DOI 10.1111/j.1365-313X.2007.03187.x
    • Kong, S. G., Kinoshita, T., Shimazaki, K., Mochizuki, N., Suzuki, T., and Nagatani, A. (2007) The C-terminal kinase fragment of Arabidopsis phototropin 2 triggers constitutive phototropin responses. Plant J. 51, 862-873 (Pubitemid 47301660)
    • (2007) Plant Journal , vol.51 , Issue.5 , pp. 862-873
    • Kong, S.-G.1    Kinoshita, T.2    Shimazaki, K.-I.3    Mochizuki, N.4    Suzuki, T.5    Nagatani, A.6
  • 19
    • 0034622586 scopus 로고    scopus 로고
    • Photochemical and mutational analysis of the FMN-binding domains of the plant blue light receptor, phototropin
    • DOI 10.1021/bi000585+
    • Salomon, M., Christie, J. M., Knieb, E., Lempert, U., and Briggs, W. R. (2000) Photochemical and mutational analysis of the FMN-binding domains of the plant blue light receptor, phototropin. Biochemistry 39, 9401-9410 (Pubitemid 30626330)
    • (2000) Biochemistry , vol.39 , Issue.31 , pp. 9401-9410
    • Salomon, M.1    Christie, J.M.2    Knieb, E.3    Lempert, U.4    Briggs, W.R.5
  • 21
    • 0036016438 scopus 로고    scopus 로고
    • Photoexcited structure of a plant photoreceptor domain reveals a light-driven molecular switch
    • DOI 10.1105/tpc.010475
    • Crosson, S., and Moffat, K. (2002) Photoexcited structure of a plant photoreceptor domain reveals a light-driven molecular switch. Plant Cell 14, 1067-1075 (Pubitemid 34609217)
    • (2002) Plant Cell , vol.14 , Issue.5 , pp. 1067-1075
    • Crosson, S.1    Moffat, K.2
  • 22
    • 37049002915 scopus 로고    scopus 로고
    • N- and C-terminal flanking regions modulate light-induced signal transduction in the LOV2 domain of the blue light sensor phototropin 1 from Avena sativa
    • DOI 10.1021/bi701543e
    • Halavaty, A. S., and Moffat, K. (2007) N- and C-terminal flanking regions modulate light-induced signal transduction in the LOV2 domain of the blue light sensor phototropin 1 from Avena sativa. Biochemistry 46, 14001-14009 (Pubitemid 350250297)
    • (2007) Biochemistry , vol.46 , Issue.49 , pp. 14001-14009
    • Halavaty, A.S.1    Moffat, K.2
  • 23
    • 0036776294 scopus 로고    scopus 로고
    • Phototropin LOV domains exhibit distinct roles in regulating photoreceptor function
    • DOI 10.1046/j.1365-313X.2002.01415.x
    • Christie, J. M., Swartz, T. E., Bogomolni, R. A., and Briggs, W. R. (2002) Phototropin LOV domains exhibit distinct roles in regulating photoreceptor function. Plant J. 32, 205-219 (Pubitemid 35249919)
    • (2002) Plant Journal , vol.32 , Issue.2 , pp. 205-219
    • Christie, J.M.1    Swartz, T.E.2    Bogomolni, R.A.3    Briggs, W.R.4
  • 24
    • 33846377245 scopus 로고    scopus 로고
    • Physiological roles of the light, oxygen, or voltage domains of phototropin 1 and phototropin 2 in arabidopsis
    • DOI 10.1104/pp.106.089839
    • Cho, H. Y., Tseng, T. S., Kaiserli, E., Sullivan, S., Christie, J. M., and Briggs, W. R. (2007) Physiological roles of the light, oxygen, or voltage domains of phototropin 1 and phototropin 2 in Arabidopsis. Plant Physiol. 143, 517-529 (Pubitemid 46133654)
    • (2007) Plant Physiology , vol.143 , Issue.1 , pp. 517-529
    • Cho, H.-Y.1    Tseng, T.-S.2    Kaiserli, E.3    Sullivan, S.4    Christie, J.M.5    Briggs, W.R.6
  • 25
    • 0141707094 scopus 로고    scopus 로고
    • Structural basis of a phototropin light switch
    • DOI 10.1126/science.1086810
    • Harper, S. M., Neil, L. C., and Gardner, K. H. (2003) Structural basis of a phototropin light switch. Science 301, 1541-1544 (Pubitemid 37128547)
    • (2003) Science , vol.301 , Issue.5639 , pp. 1541-1544
    • Harper, S.M.1    Neil, L.C.2    Gardner, K.H.3
  • 26
    • 34247184631 scopus 로고    scopus 로고
    • A LOV story: The signaling state of the phot1 LOV2 photocycle involves chromophore-triggered protein structure relaxation, as probed by far-UV time-resolved optical rotatory dispersion spectroscopy
    • DOI 10.1021/bi602544n
    • Chen, E., Swartz, T. E., Bogomolni, R. A., and Kliger, D. S. (2007) A LOV story: the signaling state of the phot1 LOV2 photocycle involves chromophore-triggered protein structure relaxation, as probed by far-UV time-resolved optical rotatory dispersion spectroscopy. Biochemistry 46, 4619-4624 (Pubitemid 46625517)
    • (2007) Biochemistry , vol.46 , Issue.15 , pp. 4619-4624
    • Chen, E.1    Swartz, T.E.2    Bogomolni, R.A.3    Kliger, D.S.4
  • 27
    • 67649312242 scopus 로고    scopus 로고
    • Light signal transduction pathway from flavin chromophore to the Jα helix of Arabidopsis phototropin1
    • Yamamoto, A., Iwata, T., Sato, Y., Matsuoka, D., Tokutomi, S., and Kandori, H. (2009) Light signal transduction pathway from flavin chromophore to the Jα helix of Arabidopsis phototropin1. Biophys. J. 96, 2771-2778
    • (2009) Biophys. J. , vol.96 , pp. 2771-2778
    • Yamamoto, A.1    Iwata, T.2    Sato, Y.3    Matsuoka, D.4    Tokutomi, S.5    Kandori, H.6
  • 28
    • 11144344967 scopus 로고    scopus 로고
    • Disruption of the LOV-Jα helix interaction activates phototropin kinase activity
    • DOI 10.1021/bi048092i
    • Harper, S. M., Christie, J. M., and Gardner, K. H. (2004) Disruption of the LOV-Jα helix interaction activates phototropin kinase activity. Biochemistry 43, 16184-16192 (Pubitemid 40041031)
    • (2004) Biochemistry , vol.43 , Issue.51 , pp. 16184-16192
    • Harper, S.M.1    Christie, J.M.2    Gardner, K.H.3
  • 29
    • 79951619904 scopus 로고    scopus 로고
    • Light-induced movement of the LOV2 domain in an Asp720Asn mutant LOV2-kinase fragment of Arabidopsis phototropin 2
    • Takayama, Y., Nakasako, M., Okajima, K., Iwata, A., Kashojiya, S., Matsui, Y., and Tokutomi, S. (2011) Light-induced movement of the LOV2 domain in an Asp720Asn mutant LOV2-kinase fragment of Arabidopsis phototropin 2. Biochemistry 50, 1174-1183
    • (2011) Biochemistry , vol.50 , pp. 1174-1183
    • Takayama, Y.1    Nakasako, M.2    Okajima, K.3    Iwata, A.4    Kashojiya, S.5    Matsui, Y.6    Tokutomi, S.7
  • 30
    • 34547867804 scopus 로고    scopus 로고
    • Steric interactions stabilize the signaling state of the LOV2 domain of phototropin 1
    • DOI 10.1021/bi700852w
    • Christie, J. M., Corchnoy, S. B., Swartz, T. E., Hokenson, M., Han, I. S., Briggs, W. R., and Bogomolni, R. A. (2007) Steric interactions stabilize the signaling state of the LOV2 domain of phototropin 1. Biochemistry 46, 9310-9319 (Pubitemid 47255043)
    • (2007) Biochemistry , vol.46 , Issue.32 , pp. 9310-9319
    • Christie, J.M.1    Corchnoy, S.B.2    Swartz, T.E.3    Hokenson, M.4    Han, I.-S.5    Briggs, W.R.6    Bogomolni, R.A.7
  • 32
    • 44949237144 scopus 로고    scopus 로고
    • Protein kinases Fpk1p and Fpk2p are novel regulators of phospholipid asymmetry
    • DOI 10.1091/mbc.E07-07-0646
    • Nakano, K., Yamamoto, T., Kishimoto, T., Noji, T., and Tanaka, K. (2008) Protein kinases Fpk1p and Fpk2p are novel regulators of phospholipid asymmetry. Mol. Biol. Cell 19, 1783-1797 (Pubitemid 351805129)
    • (2008) Molecular Biology of the Cell , vol.19 , Issue.4 , pp. 1783-1797
    • Nakano, K.1    Yamamoto, T.2    Kishimoto, T.3    Noji, T.4    Tanaka, K.5
  • 33
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S., and Hieter, P. (1989) A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19-27
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 34
    • 0034733591 scopus 로고    scopus 로고
    • Rapid and reliable protein extraction from yeast
    • Kushnirov, V. V. (2000) Rapid and reliable protein extraction from yeast. Yeast 16, 857-860
    • (2000) Yeast , vol.16 , pp. 857-860
    • Kushnirov, V.V.1
  • 35
    • 80255137234 scopus 로고    scopus 로고
    • LOV2-linker-kinase phosphorylates LOV1-containing N-terminal polypeptide substrate via photoreaction of LOV2 in Arabidopsis phototropin1
    • Okajima, K., Matsuoka, D., and Tokutomi, S. (2011) LOV2-linker-kinase phosphorylates LOV1-containing N-terminal polypeptide substrate via photoreaction of LOV2 in Arabidopsis phototropin1. FEBS Lett. 585, 3391-3395
    • (2011) FEBS Lett. , vol.585 , pp. 3391-3395
    • Okajima, K.1    Matsuoka, D.2    Tokutomi, S.3
  • 36
    • 3042728119 scopus 로고    scopus 로고
    • Cdc50p, a protein required for polarized growth, associates with the Drs2p P-type ATPase implicated in phospholipid translocation in Saccharomyces cerevisiae
    • DOI 10.1091/mbc.E03-11-0829
    • Saito, K., Fujimura-Kamada, K., Furuta, N., Kato, U., Umeda, M., and Tanaka, K. (2004) Cdc50p, a protein required for polarized growth, associates with the Drs2p P-type ATPase implicated in phospholipid translocation in Saccharomyces cerevisiae. Mol. Biol. Cell 15, 3418-3432 (Pubitemid 38850134)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.7 , pp. 3418-3432
    • Saito, K.1    Fujimura-Kamada, K.2    Futura, N.3    Kato, U.4    Umeda, M.5    Tanaka, K.6
  • 37
    • 33749531732 scopus 로고    scopus 로고
    • Roles for the Drs2p-Cdc50p complex in protein transport and phosphatidylserine asymmetry of the yeast plasma membrane
    • DOI 10.1111/j.1600-0854.2006.00485.x
    • Chen, S., Wang, J., Muthusamy, B. P., Liu, K., Zare, S., Andersen, R. J., and Graham, T. R. (2006) Roles for the Drs2p-Cdc50p complex in protein transport and phosphatidylserine asymmetry of the yeast plasma membrane. Traffic 7, 1503-1517 (Pubitemid 44524523)
    • (2006) Traffic , vol.7 , Issue.11 , pp. 1503-1517
    • Chen, S.1    Wang, J.2    Muthusamy, B.-P.3    Liu, K.4    Zare, S.5    Andersen, R.J.6    Graham, T.R.7
  • 38
    • 0037345029 scopus 로고    scopus 로고
    • Drs2p-related P-type ATPases Dnflp and Dnf2p are required for phospholipid translocation across the yeast plasma membrane and serve a role in endocytosis
    • DOI 10.1091/mbc.E02-08-0501
    • Pomorski, T., Lombardi, R., Riezman, H., Devaux, P. F., van Meer, G., and Holthuis, J. C. (2003) Drs2p-related P-type ATPases Dnf1p and Dnf2p are required for phospholipid translocation across the yeast plasma membrane and serve a role in endocytosis. Mol. Biol. Cell 14, 1240-1254 (Pubitemid 36337466)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.3 , pp. 1240-1254
    • Pomorski, T.1    Lombardi, R.2    Riezman, H.3    Devaux, P.F.4    Van Meer, G.5    Holthuis, J.C.M.6
  • 39
    • 33644780746 scopus 로고    scopus 로고
    • Blue light-induced association of phototropin 2 with the Golgi apparatus
    • DOI 10.1111/j.1365-313X.2006.02667.x
    • Kong, S. G., Suzuki, T., Tamura, K., Mochizuki, N., Hara-Nishimura, I., and Nagatani, A. (2006) Blue light-induced association of phototropin 2 with the Golgi apparatus. Plant J. 45, 994-1005 (Pubitemid 43344760)
    • (2006) Plant Journal , vol.45 , Issue.6 , pp. 994-1005
    • Kong, S.-G.1    Suzuki, T.2    Tamura, K.3    Mochizuki, N.4    Hara-Nishimura, I.5    Nagatani, A.6
  • 40
    • 41349122756 scopus 로고    scopus 로고
    • Phototropin receptor kinase activation by blue light
    • Jones, M. A., and Christie, J. M. (2008) Phototropin receptor kinase activation by blue light. Plant Signal. Behav. 3, 44-46 (Pubitemid 351448580)
    • (2008) Plant Signaling and Behavior , vol.3 , Issue.1 , pp. 44-46
    • Jones, M.A.1    Christie, J.M.2
  • 41
    • 34250345266 scopus 로고    scopus 로고
    • Mutational analysis of phototropin 1 provides insights into the mechanism underlying LOV2 signal transmission
    • DOI 10.1074/jbc.M605969200
    • Jones, M. A., Feeney, K. A., Kelly, S. M., and Christie, J. M. (2007) Mutational analysis of phototropin 1 provides insights into the mechanism underlying LOV2 signal transmission. J. Biol. Chem. 282, 6405-6414 (Pubitemid 47100883)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.9 , pp. 6405-6414
    • Jones, M.A.1    Feeney, K.A.2    Kelly, S.M.3    Christie, J.M.4
  • 42
    • 23244463204 scopus 로고    scopus 로고
    • The phot LOV2 domain and its interaction with LOV1
    • DOI 10.1529/biophysj.104.058230
    • Guo, H., Kottke, T., Hegemann, P., and Dick, B. (2005) The phot LOV2 domain and its interaction with LOV1. Biophys. J. 89, 402-412 (Pubitemid 41098295)
    • (2005) Biophysical Journal , vol.89 , Issue.1 , pp. 402-412
    • Guo, H.1    Kottke, T.2    Hegemann, P.3    Dick, B.4
  • 43
    • 9744263917 scopus 로고    scopus 로고
    • Light-induced structural changes of LOV domain-containing polypeptides from Arabidopsis phototropin 1 and 2 studied by small-angle X-ray scattering
    • DOI 10.1021/bi0485530
    • Nakasako, M., Iwata, T., Matsuoka, D., and Tokutomi, S. (2004) Light-induced structural changes of LOV domain-containing polypeptides from Arabidopsis phototropin 1 and 2 studied by small-angle x-ray scattering. Biochemistry 43, 14881-14890 (Pubitemid 39587464)
    • (2004) Biochemistry , vol.43 , Issue.47 , pp. 14881-14890
    • Nakasako, M.1    Iwata, T.2    Matsuoka, D.3    Tokutomi, S.4
  • 44
    • 4143081643 scopus 로고    scopus 로고
    • Dimerization of the plant photoreceptor phototropin is probably mediated by the LOV1 domain
    • DOI 10.1016/j.febslet.2004.06.081, PII S001457930400852X
    • Salomon, M., Lempert, U., and Rüdiger, W. (2004) Dimerization of the plant photoreceptor phototropin is probably mediated by the LOV1 domain. FEBS Lett. 572, 8-10 (Pubitemid 39092504)
    • (2004) FEBS Letters , vol.572 , Issue.1-3 , pp. 8-10
    • Salomon, M.1    Lempert, U.2    Rudiger, W.3
  • 45
    • 47849125383 scopus 로고    scopus 로고
    • Structural basis of the LOV1 dimerization of Arabidopsis phototropins 1 and 2
    • Nakasako, M., Zikihara, K., Matsuoka, D., Katsura, H., and Tokutomi, S. (2008) Structural basis of the LOV1 dimerization of Arabidopsis phototropins 1 and 2. J. Mol. Biol. 381, 718-733
    • (2008) J. Mol. Biol. , vol.381 , pp. 718-733
    • Nakasako, M.1    Zikihara, K.2    Matsuoka, D.3    Katsura, H.4    Tokutomi, S.5
  • 46
    • 75749099373 scopus 로고    scopus 로고
    • Blue light induces global and localized conformational changes in the kinase domain of full-length phototropin
    • Pfeifer, A., Mathes, T., Lu, Y., Hegemann, P., and Kottke, T. (2010) Blue light induces global and localized conformational changes in the kinase domain of full-length phototropin. Biochemistry 49, 1024-1032
    • (2010) Biochemistry , vol.49 , pp. 1024-1032
    • Pfeifer, A.1    Mathes, T.2    Lu, Y.3    Hegemann, P.4    Kottke, T.5
  • 48
    • 54349128912 scopus 로고    scopus 로고
    • Blue light induced interaction of LOV domains from Chlamydomonas reinhardtii
    • Kutta, R. J., Hofinger, E. S., Preuss, H., Bernhardt, G., and Dick, B. (2008) Blue light induced interaction of LOV domains from Chlamydomonas reinhardtii. ChemBioChem 9, 1931-1938
    • (2008) ChemBioChem , vol.9 , pp. 1931-1938
    • Kutta, R.J.1    Hofinger, E.S.2    Preuss, H.3    Bernhardt, G.4    Dick, B.5
  • 49
    • 58849158421 scopus 로고    scopus 로고
    • A conserved glutamine plays a central role in LOV domain signal transmission and its duration
    • Nash, A. I., Ko, W. H., Harper, S. M., and Gardner, K. H. (2008) A conserved glutamine plays a central role in LOV domain signal transmission and its duration. Biochemistry 47, 13842-13849
    • (2008) Biochemistry , vol.47 , pp. 13842-13849
    • Nash, A.I.1    Ko, W.H.2    Harper, S.M.3    Gardner, K.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.