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Volumn 49, Issue 41, 2010, Pages 8882-8891

Key dynamics of conserved asparagine in a cryptochrome/photolyase family protein by Fourier transform infrared spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CARBOXYLIC ACIDS; FOURIER TRANSFORM INFRARED SPECTROSCOPY; MAMMALS; PLANTS (BOTANY); PROTEINS;

EID: 77957904119     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi1009979     Document Type: Article
Times cited : (35)

References (57)
  • 1
    • 33744587947 scopus 로고    scopus 로고
    • The cryptochromes
    • Article 220
    • Lin, C. and Todo, T. (2005) The cryptochromes Genome Biol. 6 Article 220
    • (2005) Genome Biol. , vol.6
    • Lin, C.1    Todo, T.2
  • 2
    • 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, 2203-2237
    • (2003) Chem. Rev. , vol.103 , pp. 2203-2237
    • Sancar, A.1
  • 3
    • 0141762747 scopus 로고    scopus 로고
    • Cryptochromes: Enabling plants and animals to determine circadian time
    • Cashmore, A. R. (2003) Cryptochromes: Enabling plants and animals to determine circadian time Cell 114, 537-543
    • (2003) Cell , vol.114 , pp. 537-543
    • Cashmore, A.R.1
  • 6
    • 0034660609 scopus 로고    scopus 로고
    • Bacterial cryptochrome and photolyase: Characterization of two photolyase-like genes of Synechocystis sp. PCC6803
    • Hitomi, K., Okamoto, K., Daiyasu, H., Miyashita, H., Iwai, S., Toh, H., Ishiura, M., and Todo, T. (2000) Bacterial cryptochrome and photolyase: Characterization of two photolyase-like genes of Synechocystis sp. PCC6803 Nucleic Acids Res. 28, 2353-2362
    • (2000) Nucleic Acids Res. , vol.28 , pp. 2353-2362
    • Hitomi, K.1    Okamoto, K.2    Daiyasu, H.3    Miyashita, H.4    Iwai, S.5    Toh, H.6    Ishiura, M.7    Todo, T.8
  • 9
    • 33750713440 scopus 로고    scopus 로고
    • A cryptochrome/photolyase class of enzymes with single-stranded DNA-specific photolyase activity
    • Selby, C. P. and Sancar, A. (2006) A cryptochrome/photolyase class of enzymes with single-stranded DNA-specific photolyase activity Proc. Natl. Acad. Sci. U.S.A. 103, 17696-17700
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 17696-17700
    • Selby, C.P.1    Sancar, A.2
  • 11
    • 67349187333 scopus 로고    scopus 로고
    • Diatom PtCPF1 is a new cryptochrome/photolyase family member with DNA repair and transcription regulation activity
    • Coesel, S., Mangogna, M., Ishikawa, T., Heijde, M., Rogato, A., Finazzi, G., Todo, T., Bowler, C., and Falciatore, A. (2009) Diatom PtCPF1 is a new cryptochrome/photolyase family member with DNA repair and transcription regulation activity EMBO Rep. 10, 655-661
    • (2009) EMBO Rep. , vol.10 , pp. 655-661
    • Coesel, S.1    Mangogna, M.2    Ishikawa, T.3    Heijde, M.4    Rogato, A.5    Finazzi, G.6    Todo, T.7    Bowler, C.8    Falciatore, A.9
  • 13
    • 33845189961 scopus 로고    scopus 로고
    • Crystal structure of cryptochrome 3 from Arabidopsis thaliana and its implication for photolyase activity
    • Huang, Y., Baxter, R., Smith, B. S., Partch, C. L., Colbert, C. L., and Deisenhofer, J. (2006) Crystal structure of cryptochrome 3 from Arabidopsis thaliana and its implication for photolyase activity Proc. Natl. Acad. Sci. U.S.A. 103, 17701-17706
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 17701-17706
    • Huang, Y.1    Baxter, R.2    Smith, B.S.3    Partch, C.L.4    Colbert, C.L.5    Deisenhofer, J.6
  • 14
    • 52149085899 scopus 로고    scopus 로고
    • Involvement of electron transfer in the photoreaction of zebrafish cryptochrome-DASH
    • Zikihara, K., Ishikawa, T., Todo, T., and 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
  • 16
    • 73149114186 scopus 로고    scopus 로고
    • Kinetic stability of the flavin semiquinone in photolyase and cryptochrome-DASH
    • Damiani, M. J., Yalloway, G. N., Lu, J., McLeod, N. R., and O'Neill, M. A. (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
  • 18
    • 0023643412 scopus 로고
    • The active form of Escherichia coli DNA photolyase contains a fully reduced flavin and not a flavin radical, both in vivo and in vitro
    • Payne, G., Heelis, P. F., Rohrs, B. R., and Sancar, A. (1987) The active form of Escherichia coli DNA photolyase contains a fully reduced flavin and not a flavin radical, both in vivo and in vitro Biochemistry 26, 7121-7127
    • (1987) Biochemistry , vol.26 , pp. 7121-7127
    • Payne, G.1    Heelis, P.F.2    Rohrs, B.R.3    Sancar, A.4
  • 19
    • 34250346126 scopus 로고    scopus 로고
    • A novel photoreaction mechanism for the circadian blue light photoreceptor Drosophila cryptochrome
    • Berndt, A., Kottke, T., Breitkreuz, H., Dvorsky, R., Hennig, S., Alexander, M., and Wolf, E. (2007) A novel photoreaction mechanism for the circadian blue light photoreceptor Drosophila cryptochrome J. Biol. Chem. 282, 13011-13021
    • (2007) J. Biol. Chem. , vol.282 , pp. 13011-13021
    • Berndt, A.1    Kottke, T.2    Breitkreuz, H.3    Dvorsky, R.4    Hennig, S.5    Alexander, M.6    Wolf, E.7
  • 21
    • 0034622586 scopus 로고    scopus 로고
    • Photochemical and mutational analysis of the FMN-binding domains of the plant blue light receptor, phototropin
    • 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
    • (2000) Biochemistry , vol.39 , pp. 9401-9410
    • Salomon, M.1    Christie, J.M.2    Knieb, E.3    Lempert, U.4    Briggs, W.R.5
  • 24
    • 0036016438 scopus 로고    scopus 로고
    • Photoexcited structure of a plant photoreceptor domain reveals a light-driven molecular switch
    • Crosson, S. and Moffat, K. (2002) Photoexcited structure of a plant photoreceptor domain reveals a light-driven molecular switch Plant Cell 14, 1067-1075
    • (2002) Plant Cell , vol.14 , pp. 1067-1075
    • Crosson, S.1    Moffat, K.2
  • 25
    • 3142617400 scopus 로고    scopus 로고
    • Role of Gln1029 in the photoactivation processes of the LOV2 domain in Adiantum phytochrome3
    • Nozaki, D., Iwata, T., Ishikawa, T., Todo, T., Tokutomi, S., and Kandori, H. (2004) Role of Gln1029 in the photoactivation processes of the LOV2 domain in Adiantum phytochrome3 Biochemistry 43, 8373-8379
    • (2004) Biochemistry , vol.43 , pp. 8373-8379
    • Nozaki, D.1    Iwata, T.2    Ishikawa, T.3    Todo, T.4    Tokutomi, S.5    Kandori, H.6
  • 26
    • 0037489440 scopus 로고    scopus 로고
    • Light-induced structural changes in the LOV2 domain of Adiantum phytochrome3 studied by low-temperature FTIR and UV-visible spectroscopy
    • Iwata, T., Nozaki, D., Tokutomi, S., Kagawa, T., Wada, M., and Kandori, H. (2003) Light-induced structural changes in the LOV2 domain of Adiantum phytochrome3 studied by low-temperature FTIR and UV-visible spectroscopy Biochemistry 42, 8183-8191
    • (2003) Biochemistry , vol.42 , pp. 8183-8191
    • Iwata, T.1    Nozaki, D.2    Tokutomi, S.3    Kagawa, T.4    Wada, M.5    Kandori, H.6
  • 27
    • 11144344967 scopus 로고    scopus 로고
    • Disruption of the LOV-Jα helix interaction activates phototropin kinase activity
    • 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
    • (2004) Biochemistry , vol.43 , pp. 16184-16192
    • Harper, S.M.1    Christie, J.M.2    Gardner, K.H.3
  • 28
    • 34250345266 scopus 로고    scopus 로고
    • Mutational analysis of phototropin 1 provides insights into the mechanism underlying LOV2 signal transmission
    • 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
    • (2007) J. Biol. Chem. , vol.282 , pp. 6405-6414
    • Jones, M.A.1    Feeney, K.A.2    Kelly, S.M.3    Christie, J.M.4
  • 29
    • 67649312242 scopus 로고    scopus 로고
    • Light signal transduction pathway from flavin chromophore to 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 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
  • 30
    • 18144372698 scopus 로고    scopus 로고
    • Structure of cyanobacterial BLUF protein, Tll0078, containing a novel FAD-binding blue light sensor domain
    • Kita, A., Okajima, K., Morimoto, Y., Ikeuchi, M., and Miki, K. (2005) Structure of cyanobacterial BLUF protein, Tll0078, containing a novel FAD-binding blue light sensor domain J. Mol. Biol. 349, 1-5
    • (2005) J. Mol. Biol. , vol.349 , pp. 1-5
    • Kita, A.1    Okajima, K.2    Morimoto, Y.3    Ikeuchi, M.4    Miki, K.5
  • 31
    • 25444486111 scopus 로고    scopus 로고
    • Photocycle features of heterologously expressed and assembled eukaryotic flavin-binding BLUF domains of photoactivated adenylyl cyclase (PAC), a blue-light receptor in Euglena gracilis
    • Ito, S., Murakami, A., Sato, K., Nishina, Y., Shiga, K., Takahashi, T., Higashi, S., Iseki, M., and Watanabe, M. (2005) Photocycle features of heterologously expressed and assembled eukaryotic flavin-binding BLUF domains of photoactivated adenylyl cyclase (PAC), a blue-light receptor in Euglena gracilis Photochem. Photobiol. Sci. 4, 762-769
    • (2005) Photochem. Photobiol. Sci. , vol.4 , pp. 762-769
    • Ito, S.1    Murakami, A.2    Sato, K.3    Nishina, Y.4    Shiga, K.5    Takahashi, T.6    Higashi, S.7    Iseki, M.8    Watanabe, M.9
  • 33
    • 62849120822 scopus 로고    scopus 로고
    • What makes the difference between a cryptochrome and DNA photolyase? A spectroelectrochemical comparison of the flavin redox transitions
    • Balland, V., Byrdin, M., Eker, A. P. M., Ahmad, M., and Brettel, K. (2009) What makes the difference between a cryptochrome and DNA photolyase? A spectroelectrochemical comparison of the flavin redox transitions J. Am. Chem. Soc. 131, 426-427
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 426-427
    • Balland, V.1    Byrdin, M.2    Eker, A.P.M.3    Ahmad, M.4    Brettel, K.5
  • 34
    • 49749112845 scopus 로고    scopus 로고
    • Active site of Escherichia coli DNA photolyase: Asn378 is crucial both for stabilizing the neutral flavin radical cofactor and for DNA repair
    • Xu, L., Mu, W., Ding, Y., Luo, Z., Han, Q., Bi, F., Wang, Y., and Song, Y. (2008) Active site of Escherichia coli DNA photolyase: Asn378 is crucial both for stabilizing the neutral flavin radical cofactor and for DNA repair Biochemistry 47, 8736-8743
    • (2008) Biochemistry , vol.47 , pp. 8736-8743
    • Xu, L.1    Mu, W.2    Ding, Y.3    Luo, Z.4    Han, Q.5    Bi, F.6    Wang, Y.7    Song, Y.8
  • 36
    • 0028909764 scopus 로고
    • Infrared spectroscopy applied to biochemical and biological problems
    • Siebert, F. (1995) Infrared spectroscopy applied to biochemical and biological problems Methods Enzymol. 246, 501-526
    • (1995) Methods Enzymol. , vol.246 , pp. 501-526
    • Siebert, F.1
  • 37
    • 0034734254 scopus 로고    scopus 로고
    • Role of internal water molecules in bacteriorhodopsin
    • Kandori, H. (2000) Role of internal water molecules in bacteriorhodopsin Biochim. Biophys. Acta 1460, 177-191
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 177-191
    • Kandori, H.1
  • 38
    • 3543020365 scopus 로고    scopus 로고
    • Hydrogen switch model for the proton transfer in the Schiff base region of bacteriorhodopsin
    • Kandori, H. (2004) Hydrogen switch model for the proton transfer in the Schiff base region of bacteriorhodopsin Biochim. Biophys. Acta 1658, 72-79
    • (2004) Biochim. Biophys. Acta , vol.1658 , pp. 72-79
    • Kandori, H.1
  • 39
    • 17444409955 scopus 로고    scopus 로고
    • Light-induced reactions of Escherichia coli DNA photolyase monitored by Fourier transform infrared spectroscopy
    • Schleicher, E., Hesssling, B., Illarionova, V., Bacher, A., Weber, S., Richter, G., and Gerwert, K. (2005) Light-induced reactions of Escherichia coli DNA photolyase monitored by Fourier transform infrared spectroscopy FEBS J. 272, 1855-1866
    • (2005) FEBS J. , vol.272 , pp. 1855-1866
    • Schleicher, E.1    Hesssling, B.2    Illarionova, V.3    Bacher, A.4    Weber, S.5    Richter, G.6    Gerwert, K.7
  • 40
    • 33644553813 scopus 로고    scopus 로고
    • Blue-light-induced changes in Arabidopsis cryptochrome 1 probed by FTIR difference spectroscopy
    • Kottke, T., Batschauer, A., Ahmad, M., and 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
  • 41
    • 0037062577 scopus 로고    scopus 로고
    • Vibration spectroscopy reveals light-induced chromophore and protein structural changes in the LOV2 domain of the plant blue-light receptor phototropin 1
    • Swartz, T. E., Wenzel, P. J., Corchnoy, S. B., Briggs, W. R., and Bogomolni, R. A. (2002) Vibration spectroscopy reveals light-induced chromophore and protein structural changes in the LOV2 domain of the plant blue-light receptor phototropin 1 Biochemistry 41, 7183-7189
    • (2002) Biochemistry , vol.41 , pp. 7183-7189
    • Swartz, T.E.1    Wenzel, P.J.2    Corchnoy, S.B.3    Briggs, W.R.4    Bogomolni, R.A.5
  • 42
    • 0037048688 scopus 로고    scopus 로고
    • Photoreaction of the cysteine S-H group in the LOV2 domain of Adiantum phytochrome3
    • Iwata, T., Tokutomi, S., and Kandori, H. (2002) Photoreaction of the cysteine S-H group in the LOV2 domain of Adiantum phytochrome3 J. Am. Chem. Soc. 124, 11840-11841
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11840-11841
    • Iwata, T.1    Tokutomi, S.2    Kandori, H.3
  • 43
    • 12244256754 scopus 로고    scopus 로고
    • Vibrational spectroscopy of an algal phot-LOV1 domain probes the molecular changes associated with blue-light reception
    • Ataka, K., Hegemann, P., and Heberle, J. (2003) Vibrational spectroscopy of an algal phot-LOV1 domain probes the molecular changes associated with blue-light reception Biophys. J. 84, 466-474
    • (2003) Biophys. J. , vol.84 , pp. 466-474
    • Ataka, K.1    Hegemann, P.2    Heberle, J.3
  • 44
    • 18844391283 scopus 로고    scopus 로고
    • Comparative investigation of the LOV1 and LOV2 domains in Adiantum phytochrome3
    • Iwata, T., Nozaki, D., Tokutomi, S., and Kandori, H. (2005) Comparative investigation of the LOV1 and LOV2 domains in Adiantum phytochrome3 Biochemistry 44, 7427-7434
    • (2005) Biochemistry , vol.44 , pp. 7427-7434
    • Iwata, T.1    Nozaki, D.2    Tokutomi, S.3    Kandori, H.4
  • 46
    • 38349119939 scopus 로고    scopus 로고
    • Role of Phe1010 in light-induced structural changes of the neo1-LOV2 domain of Adiantum
    • Yamamoto, A., Iwata, T., Tokutomi, S., and Kandori, H. (2008) Role of Phe1010 in light-induced structural changes of the neo1-LOV2 domain of Adiantum Biochemistry 47, 922-928
    • (2008) Biochemistry , vol.47 , pp. 922-928
    • Yamamoto, A.1    Iwata, T.2    Tokutomi, S.3    Kandori, H.4
  • 47
    • 68849111523 scopus 로고    scopus 로고
    • Different Role of the Jα Helix in the Light-Induced Activation of the LOV2 Domains in Various Phototropins
    • Koyama, T., Iwata, T., Yamamoto, A., Sato, Y., Matsuoka, D., Tokutomi, S., and Kandori, H. (2009) Different Role of the Jα Helix in the Light-Induced Activation of the LOV2 Domains in Various Phototropins Biochemistry 48, 7621-7628
    • (2009) Biochemistry , vol.48 , pp. 7621-7628
    • Koyama, T.1    Iwata, T.2    Yamamoto, A.3    Sato, Y.4    Matsuoka, D.5    Tokutomi, S.6    Kandori, H.7
  • 48
    • 2442559284 scopus 로고    scopus 로고
    • Light-induced structural changes in a putative blue-light receptor with a novel FAD binding fold sense of blue-light using FAD (BLUF); Slr1694 of Synechocystis sp. PCC6803
    • Masuda, S., Hasegawa, K., Ishii, A., and Ono, T. (2004) Light-induced structural changes in a putative blue-light receptor with a novel FAD binding fold sense of blue-light using FAD (BLUF); slr1694 of Synechocystis sp. PCC6803 Biochemistry 43, 5304-5313
    • (2004) Biochemistry , vol.43 , pp. 5304-5313
    • Masuda, S.1    Hasegawa, K.2    Ishii, A.3    Ono, T.4
  • 49
    • 13444291923 scopus 로고    scopus 로고
    • Light-induced structural changes of apoprotein and chromophore in the sensor of blue light using FAD (BLUF) domain of AppA for a signaling state
    • DOI 10.1021/bi047876t
    • Masuda, S., Hasegawa, K., and Ono, T. (2005) Light-induced structural changes of apoprotein and chromophore in the sensor of blue light using FAD (BLUF) domain of AppA for a signaling state Biochemistry 44, 1215-1224 (Pubitemid 40209001)
    • (2005) Biochemistry , vol.44 , Issue.4 , pp. 1215-1224
    • Masuda, S.1    Hasegawa, K.2    Ono, T.-A.3
  • 50
    • 33645235288 scopus 로고    scopus 로고
    • Light induced structural changes of a full-length protein and its BLUF domain in YcgF (Blrp), a blue-light sensing protein that use FAD (BLUF)
    • Hasegawa, K., Masuda, S., and Ono, T. (2006) Light induced structural changes of a full-length protein and its BLUF domain in YcgF (Blrp), a blue-light sensing protein that use FAD (BLUF) Biochemistry 45, 3785-3793
    • (2006) Biochemistry , vol.45 , pp. 3785-3793
    • Hasegawa, K.1    Masuda, S.2    Ono, T.3
  • 51
    • 0019889065 scopus 로고
    • Normal mode analysis of lumiflavin and interpretation of resonance Raman spectra of flavoproteins
    • Bowman, W. D. and Spiro, T. G. (1981) Normal mode analysis of lumiflavin and interpretation of resonance Raman spectra of flavoproteins Biochemistry 20, 3313-3318
    • (1981) Biochemistry , vol.20 , pp. 3313-3318
    • Bowman, W.D.1    Spiro, T.G.2
  • 52
    • 0021094373 scopus 로고
    • Assignment and the effect of hydrogen bonding on the vibrational normal modes of flavins and flavoproteins
    • Schmidt, J., Coudron, P., Thompson, A. W., Watters, K. L., and McFarland, J. T. (1983) Assignment and the effect of hydrogen bonding on the vibrational normal modes of flavins and flavoproteins Biochemistry 22, 76-84
    • (1983) Biochemistry , vol.22 , pp. 76-84
    • Schmidt, J.1    Coudron, P.2    Thompson, A.W.3    Watters, K.L.4    McFarland, J.T.5
  • 53
    • 0001411522 scopus 로고
    • Vibrational analysis of flavin derivatives: Normal coordinate treatments of lumiflavin
    • Abe, M. and Kyogoku, Y. (1987) Vibrational analysis of flavin derivatives: Normal coordinate treatments of lumiflavin Spectrochim. Acta 43A, 1027-1038
    • (1987) Spectrochim. Acta , vol.43 , pp. 1027-1038
    • Abe, M.1    Kyogoku, Y.2
  • 54
    • 0001027209 scopus 로고
    • Assignment and the effect of hydrogen bonding on the vibrational normal modes of flavins and flavoproteins
    • Livery, C. R. and McFarland, J. T. (1990) Assignment and the effect of hydrogen bonding on the vibrational normal modes of flavins and flavoproteins J. Phys. Chem. 94, 3980-3994
    • (1990) J. Phys. Chem. , vol.94 , pp. 3980-3994
    • Livery, C.R.1    McFarland, J.T.2
  • 55
    • 0001049969 scopus 로고
    • Time-resolved SERS study of direct photochemical charge transfer between FMN and a Ag electrode
    • Zhang, W., Vivoni, A., Lombard, J. R., and Birke, R. L. (1995) Time-resolved SERS study of direct photochemical charge transfer between FMN and a Ag electrode J. Phys. Chem. 99, 12846-12857
    • (1995) J. Phys. Chem. , vol.99 , pp. 12846-12857
    • Zhang, W.1    Vivoni, A.2    Lombard, J.R.3    Birke, R.L.4


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