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Volumn 94, Issue 9, 2008, Pages 3620-3628

Diverse roles of glycine residues conserved in photoactive yellow proteins

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; BACTERIAL PROTEIN; GLYCINE; PHOTOACTIVE YELLOW PROTEIN, BACTERIA; VISUAL PROTEINS AND PIGMENTS;

EID: 43649085346     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.107.123414     Document Type: Article
Times cited : (9)

References (52)
  • 1
    • 0028577744 scopus 로고
    • Complete chemical structure of photoactive yellow protein: Novel thioester-linked 4-hydroxycinnamyl chromophore and photocycle chemistry
    • Baca, M., G. E. Borgstahl, M. Boissinot, P. M. Burke, D. R. Williams, K. A. Slater, and E. D. Getzoff. 1994. Complete chemical structure of photoactive yellow protein: novel thioester-linked 4-hydroxycinnamyl chromophore and photocycle chemistry. Biochemistry. 33:14369-14377.
    • (1994) Biochemistry , vol.33 , pp. 14369-14377
    • Baca, M.1    Borgstahl, G.E.2    Boissinot, M.3    Burke, P.M.4    Williams, D.R.5    Slater, K.A.6    Getzoff, E.D.7
  • 3
    • 0028868422 scopus 로고
    • Reconsti-tution photoactive yellow protein from apoprotein and p-coumaric acid derivatives
    • Imamoto, Y., T. Ito, M. Kataoka, and F. Tokunaga. 1995. Reconsti-tution photoactive yellow protein from apoprotein and p-coumaric acid derivatives. FEBS Lett. 374:157-160.
    • (1995) FEBS Lett , vol.374 , pp. 157-160
    • Imamoto, Y.1    Ito, T.2    Kataoka, M.3    Tokunaga, F.4
  • 4
    • 0029110488 scopus 로고
    • 1.4 Å structure of photoactive yellow protein, a cytosolic photoreceptor: Unusual fold, active site, and chromophore
    • Borgstahl, G. E., D. R. Williams, and E. D. Getzoff. 1995. 1.4 Å structure of photoactive yellow protein, a cytosolic photoreceptor: unusual fold, active site, and chromophore. Biochemistry. 34:6278-6287.
    • (1995) Biochemistry , vol.34 , pp. 6278-6287
    • Borgstahl, G.E.1    Williams, D.R.2    Getzoff, E.D.3
  • 5
    • 0043125483 scopus 로고    scopus 로고
    • Anticipatory active-site motions and chromophore distortion prime photoreceptor PYP for light activation
    • Getzoff, E. D., K. N. Gutwin, and U. K. Genick. 2003. Anticipatory active-site motions and chromophore distortion prime photoreceptor PYP for light activation. Nat. Struct. Biol. 10:663-668.
    • (2003) Nat. Struct. Biol , vol.10 , pp. 663-668
    • Getzoff, E.D.1    Gutwin, K.N.2    Genick, U.K.3
  • 6
    • 0022430790 scopus 로고
    • Isolation and characterization of soluble cyto-chromes, ferredoxins and other chromophoric proteins from the halo-philic phototrophic bacterium Ectothiorhodospira halophila
    • Meyer, T. E. 1985. Isolation and characterization of soluble cyto-chromes, ferredoxins and other chromophoric proteins from the halo-philic phototrophic bacterium Ectothiorhodospira halophila. Biochim. Biophys. Acta. 806:175-183.
    • (1985) Biochim. Biophys. Acta , vol.806 , pp. 175-183
    • Meyer, T.E.1
  • 7
    • 0037657894 scopus 로고    scopus 로고
    • Photoactive yellow protein: A prototypic PAS domain sensory protein and development of a common signaling mechanism
    • Cusanovich, M. A., and T. E. Meyer. 2003. Photoactive yellow protein: a prototypic PAS domain sensory protein and development of a common signaling mechanism. Biochemistry. 42:4759-4770.
    • (2003) Biochemistry , vol.42 , pp. 4759-4770
    • Cusanovich, M.A.1    Meyer, T.E.2
  • 9
    • 0029892214 scopus 로고    scopus 로고
    • Sequence evidence for strong conservation of the photoactive yellow proteins from the halophilic phototrophic bacteria Chromatium salexigens and Rhodo-spirillum salexigens
    • Koh, M., G. Van Driessche, B. Samyn, W. D. Hoff, T. E. Meyer, M. A. Cusanovich, and J. J. Van Beeumen. 1996. Sequence evidence for strong conservation of the photoactive yellow proteins from the halophilic phototrophic bacteria Chromatium salexigens and Rhodo-spirillum salexigens. Biochemistry. 35:2526-2534.
    • (1996) Biochemistry , vol.35 , pp. 2526-2534
    • Koh, M.1    Van Driessche, G.2    Samyn, B.3    Hoff, W.D.4    Meyer, T.E.5    Cusanovich, M.A.6    Van Beeumen, J.J.7
  • 12
    • 3242747592 scopus 로고    scopus 로고
    • Photoactive yellow protein, bacteriophytochrome, and sensory rhodopsin in purple phototrophic bacteria
    • Kyndt, J. A., T. E. Meyer, and M. A. Cusanovich. 2004. Photoactive yellow protein, bacteriophytochrome, and sensory rhodopsin in purple phototrophic bacteria. Photochem. Photobiol. Sci. 3:519-530.
    • (2004) Photochem. Photobiol. Sci , vol.3 , pp. 519-530
    • Kyndt, J.A.1    Meyer, T.E.2    Cusanovich, M.A.3
  • 13
    • 0033575370 scopus 로고    scopus 로고
    • Bacterial photoreceptor with similarity to photoactive yellow protein and plant phytochromes
    • Jiang, Z., L. R. Swem, B. G. Rushing, S. Devanathan, G. Tollin, and C. E. Bauer. 1999. Bacterial photoreceptor with similarity to photoactive yellow protein and plant phytochromes. Science. 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
  • 14
    • 0027271859 scopus 로고
    • Primary structure of a photoactive yellow protein from the phototrophic bacterium Ectothiorhodospira halophila, with evidence for the mass and the binding site of the chromophore
    • Van Beeumen, J. J., B. V. Devreese, S. M. Van Bun, W. D. Hoff, K. J. Hellingwerf, T. E. Meyer, D. E. McRee, and M. A. Cusanovich. 1993. Primary structure of a photoactive yellow protein from the phototrophic bacterium Ectothiorhodospira halophila, with evidence for the mass and the binding site of the chromophore. Protein Sci. 2:1114-1125.
    • (1993) Protein Sci , vol.2 , pp. 1114-1125
    • Van Beeumen, J.J.1    Devreese, B.V.2    Van Bun, S.M.3    Hoff, W.D.4    Hellingwerf, K.J.5    Meyer, T.E.6    McRee, D.E.7    Cusanovich, M.A.8
  • 15
    • 0030914406 scopus 로고    scopus 로고
    • Functional expression and site-directed mutagenesis of photoactive yellow protein
    • Mihara, K., O. Hisatomi, Y. Imamoto, M. Kataoka, and F. Tokunaga. 1997. Functional expression and site-directed mutagenesis of photoactive yellow protein. J. Biochem. (Tokyo). 121:876-880.
    • (1997) J. Biochem. (Tokyo) , vol.121 , pp. 876-880
    • Mihara, K.1    Hisatomi, O.2    Imamoto, Y.3    Kataoka, M.4    Tokunaga, F.5
  • 16
    • 0030589514 scopus 로고    scopus 로고
    • Phi/psi-chology: Ramachandran revisited
    • Kleywegt, G. J., and T. A. Jones. 1996. Phi/psi-chology: Ramachandran revisited. Structure. 4:1395-1400.
    • (1996) Structure , vol.4 , pp. 1395-1400
    • Kleywegt, G.J.1    Jones, T.A.2
  • 17
    • 0037155256 scopus 로고    scopus 로고
    • Engineering photocycle dynamics. Crystal structures and kinetics of three photoactive yellow protein hinge-bending mutants
    • van Aalten, D. M., A. Haker, J. Hendriks, K. J. Hellingwerf, L. Joshua-Tor, and W. Crielaard. 2002. Engineering photocycle dynamics. Crystal structures and kinetics of three photoactive yellow protein hinge-bending mutants. J. Biol. Chem. 277:6463-6468.
    • (2002) J. Biol. Chem , vol.277 , pp. 6463-6468
    • van Aalten, D.M.1    Haker, A.2    Hendriks, J.3    Hellingwerf, K.J.4    Joshua-Tor, L.5    Crielaard, W.6
  • 20
    • 0035807935 scopus 로고    scopus 로고
    • Spectro-scopic characterization of the photocycle intermediates of photoactive yellow protein
    • Imamoto, Y., K. Mihara, F. Tokunaga, and M. Kataoka. 2001. Spectro-scopic characterization of the photocycle intermediates of photoactive yellow protein. Biochemistry. 40:14336-14343.
    • (2001) Biochemistry , vol.40 , pp. 14336-14343
    • Imamoto, Y.1    Mihara, K.2    Tokunaga, F.3    Kataoka, M.4
  • 21
    • 0031808072 scopus 로고    scopus 로고
    • New photocycle intermediates in the photoactive yellow protein from Ectothiorhodospira halophila: Picosecond transient absorption spectroscopy
    • Ujj, L., S. Devanathan, T. E. Meyer, M. A. Cusanovich, G. Tollin, and G. H. Atkinson. 1998. New photocycle intermediates in the photoactive yellow protein from Ectothiorhodospira halophila: picosecond transient absorption spectroscopy. Biophys. J. 75:406-412.
    • (1998) Biophys. J , vol.75 , pp. 406-412
    • Ujj, L.1    Devanathan, S.2    Meyer, T.E.3    Cusanovich, M.A.4    Tollin, G.5    Atkinson, G.H.6
  • 22
    • 0345707600 scopus 로고    scopus 로고
    • Role of an N-terminal loop in the secondary structural change of photoactive yellow protein
    • Harigai, M., Y. Imamoto, H. Kamikubo, Y. Yamazaki, and M. Kataoka. 2003. Role of an N-terminal loop in the secondary structural change of photoactive yellow protein. Biochemistry. 42:13893-13900.
    • (2003) Biochemistry , vol.42 , pp. 13893-13900
    • Harigai, M.1    Imamoto, Y.2    Kamikubo, H.3    Yamazaki, Y.4    Kataoka, M.5
  • 23
    • 0035814881 scopus 로고    scopus 로고
    • Light induces destabilization of photoactive yellow protein
    • Ohishi, S., N. Shimizu, K. Mihara, Y. Imamoto, and M. Kataoka. 2001. Light induces destabilization of photoactive yellow protein. Biochemistry. 40:2854-2859.
    • (2001) Biochemistry , vol.40 , pp. 2854-2859
    • Ohishi, S.1    Shimizu, N.2    Mihara, K.3    Imamoto, Y.4    Kataoka, M.5
  • 24
    • 34248598352 scopus 로고    scopus 로고
    • Attempt to simplify the amino-acid sequence of photoactive yellow protein with a set of simple rules
    • Shirai, K., Y. Yamazaki, H. Kamikubo, Y. Imamoto, and M. Kataoka. 2007. Attempt to simplify the amino-acid sequence of photoactive yellow protein with a set of simple rules. Proteins. 67:821-833.
    • (2007) Proteins , vol.67 , pp. 821-833
    • Shirai, K.1    Yamazaki, Y.2    Kamikubo, H.3    Imamoto, Y.4    Kataoka, M.5
  • 25
    • 0037465835 scopus 로고    scopus 로고
    • Site-specific mutations provide new insights into the origin of pH effects and alternative spectral forms in the photoactive yellow protein from Halorhodospira halophila
    • Meyer, T. E., S. Devanathan, T. Woo, E. D. Getzoff, G. Tollin, and M. A. Cusanovich. 2003. Site-specific mutations provide new insights into the origin of pH effects and alternative spectral forms in the photoactive yellow protein from Halorhodospira halophila. Biochemistry. 42:3319-3325.
    • (2003) Biochemistry , vol.42 , pp. 3319-3325
    • Meyer, T.E.1    Devanathan, S.2    Woo, T.3    Getzoff, E.D.4    Tollin, G.5    Cusanovich, M.A.6
  • 26
    • 0030069979 scopus 로고    scopus 로고
    • Chemical reactivity and spectroscopy of the thiol ester-linked p-coumaric acid chromophore in the photoactive yellow protein from Ectothiorhodo-spira halophila
    • Hoff, W. D., B. Devreese, R. Fokkens, I. M. Nugteren-Roodzant, J. Van Beeumen, N. Nibbering, and K. J. Hellingwerf. 1996. Chemical reactivity and spectroscopy of the thiol ester-linked p-coumaric acid chromophore in the photoactive yellow protein from Ectothiorhodo-spira halophila. Biochemistry. 35:1274-1281.
    • (1996) Biochemistry , vol.35 , pp. 1274-1281
    • Hoff, W.D.1    Devreese, B.2    Fokkens, R.3    Nugteren-Roodzant, I.M.4    Van Beeumen, J.5    Nibbering, N.6    Hellingwerf, K.J.7
  • 27
    • 7544223280 scopus 로고    scopus 로고
    • Direct observation of the pH-dependent equilibrium between L-like and M intermediates of photoactive yellow protein
    • Imamoto, Y., M. Harigai, and M. Kataoka. 2004. Direct observation of the pH-dependent equilibrium between L-like and M intermediates of photoactive yellow protein. FEBS Lett. 577:75-80.
    • (2004) FEBS Lett , vol.577 , pp. 75-80
    • Imamoto, Y.1    Harigai, M.2    Kataoka, M.3
  • 28
    • 0023152468 scopus 로고
    • Properties of a water-soluble, yellow protein isolated from a halophilic phototrophic bacterium that has photochemical activity analogous to sensory rhodopsin
    • Meyer, T. E., E. Yakali, M. A. Cusanovich, and G. Tollin. 1987. Properties of a water-soluble, yellow protein isolated from a halophilic phototrophic bacterium that has photochemical activity analogous to sensory rhodopsin. Biochemistry. 26:418-423.
    • (1987) Biochemistry , vol.26 , pp. 418-423
    • Meyer, T.E.1    Yakali, E.2    Cusanovich, M.A.3    Tollin, G.4
  • 29
    • 33645224079 scopus 로고    scopus 로고
    • pH-dependent equilibrium between long lived near-UV intermediates of photoactive yellow protein
    • Shimizu, N., Y. Imamoto, M. Harigai, H. Kamikubo, Y. Yamazaki, and M. Kataoka. 2006. pH-dependent equilibrium between long lived near-UV intermediates of photoactive yellow protein. J. Biol. Chem. 281:4318-4325.
    • (2006) J. Biol. Chem , vol.281 , pp. 4318-4325
    • Shimizu, N.1    Imamoto, Y.2    Harigai, M.3    Kamikubo, H.4    Yamazaki, Y.5    Kataoka, M.6
  • 30
    • 0032568630 scopus 로고    scopus 로고
    • Photoactive yellow protein: A structural prototype for the three-dimensional fold of the PAS domain superfamily
    • Pellequer, J. L., K. A. Wager-Smith, S. A. Kay, and E. D. Getzoff. 1998. Photoactive yellow protein: a structural prototype for the three-dimensional fold of the PAS domain superfamily. Proc. Natl. Acad. Sci. USA. 95:5884-5890.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5884-5890
    • Pellequer, J.L.1    Wager-Smith, K.A.2    Kay, S.A.3    Getzoff, E.D.4
  • 31
  • 32
    • 0035906913 scopus 로고    scopus 로고
    • The role of the N-terminal domain of photoactive yellow protein in the transient partial unfolding during signalling state formation
    • van der Horst, M. A., I. H. van Stokkum, W. Crielaard, and K. J. Hellingwerf. 2001. The role of the N-terminal domain of photoactive yellow protein in the transient partial unfolding during signalling state formation. FEBS Lett. 497:26-30.
    • (2001) FEBS Lett , vol.497 , pp. 26-30
    • van der Horst, M.A.1    van Stokkum, I.H.2    Crielaard, W.3    Hellingwerf, K.J.4
  • 33
    • 0028832513 scopus 로고
    • Resonance Raman evidence that the thioester-linked 4-hydroxycin-namyl chromophore of photoactive yellow protein is deprotonated
    • Kim, M., R. A. Mathies, W. D. Hoff, and K. J. Hellingwerf. 1995. Resonance Raman evidence that the thioester-linked 4-hydroxycin-namyl chromophore of photoactive yellow protein is deprotonated. Biochemistry. 34:12669-12672.
    • (1995) Biochemistry , vol.34 , pp. 12669-12672
    • Kim, M.1    Mathies, R.A.2    Hoff, W.D.3    Hellingwerf, K.J.4
  • 34
    • 0031011485 scopus 로고    scopus 로고
    • Evidence for proton transfer from Glu-46 to the chromophore during the photocycle of photoactive yellow protein
    • Imamoto, Y., K. Mihara, O. Hisatomi, M. Kataoka, F. Tokunaga, N. Bojkova, and K. Yoshihara. 1997. Evidence for proton transfer from Glu-46 to the chromophore during the photocycle of photoactive yellow protein. J. Biol. Chem. 272:12905-12908.
    • (1997) J. Biol. Chem , vol.272 , pp. 12905-12908
    • Imamoto, Y.1    Mihara, K.2    Hisatomi, O.3    Kataoka, M.4    Tokunaga, F.5    Bojkova, N.6    Yoshihara, K.7
  • 39
    • 0037452676 scopus 로고    scopus 로고
    • Crystal structure of a photoactive yellow protein from a sensor histidine kinase: Conformational variability and signal transduction
    • Rajagopal, S., and K. Moffat. 2003. Crystal structure of a photoactive yellow protein from a sensor histidine kinase: conformational variability and signal transduction. Proc. Natl. Acad. Sci. USA. 100:1649-1654.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 1649-1654
    • Rajagopal, S.1    Moffat, K.2
  • 40
    • 0035846381 scopus 로고    scopus 로고
    • Spectral tuning of photoactive yellow protein. Theoretical and experimental analysis of medium effects on the absorption spectrum of the chromophore
    • Yoda, M., H. Houjou, Y. Inoue, and M. Sakurai. 2001. Spectral tuning of photoactive yellow protein. Theoretical and experimental analysis of medium effects on the absorption spectrum of the chromophore. J. Phys. Chem. B. 105:9887-9895.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 9887-9895
    • Yoda, M.1    Houjou, H.2    Inoue, Y.3    Sakurai, M.4
  • 41
    • 0035971221 scopus 로고    scopus 로고
    • α H··O hydrogen bond of amino acid residues
    • α H··O hydrogen bond of amino acid residues. J. Biol. Chem. 276:9832-9837.
    • (2001) J. Biol. Chem , vol.276 , pp. 9832-9837
    • Scheiner, S.1    Kar, T.2    Gu, Y.3
  • 42
    • 33845952658 scopus 로고    scopus 로고
    • Weak hydrogen bonds
    • Chemistry. J. L. Atwood and J. W. Steed, editors. Marcel Dekker, New York
    • Nishio, M. 2004. Weak hydrogen bonds. In Encyclopedia of Supra-molecular Chemistry. J. L. Atwood and J. W. Steed, editors. Marcel Dekker, New York. 1576-1585.
    • (2004) Encyclopedia of Supra-molecular , pp. 1576-1585
    • Nishio, M.1
  • 43
    • 22144464025 scopus 로고    scopus 로고
    • A vibrational spectral maker for probing the hydrogen-bonding status of protonated Asp and Glu residues
    • Nie, B., J. Stutzman, and A. Xie. 2005. A vibrational spectral maker for probing the hydrogen-bonding status of protonated Asp and Glu residues. Biophys. J. 88:2833-2847.
    • (2005) Biophys. J , vol.88 , pp. 2833-2847
    • Nie, B.1    Stutzman, J.2    Xie, A.3
  • 45
    • 0035852878 scopus 로고    scopus 로고
    • Formation of a new buried charge drives a large-amplitude protein quake in photoreceptor activation
    • Xie, A., L. Kelemen, J. Hendriks, B. J. White, K. J. Hellingwerf, and W. D. Hoff. 2001. Formation of a new buried charge drives a large-amplitude protein quake in photoreceptor activation. Biochemistry. 40:1510-1517.
    • (2001) Biochemistry , vol.40 , pp. 1510-1517
    • Xie, A.1    Kelemen, L.2    Hendriks, J.3    White, B.J.4    Hellingwerf, K.J.5    Hoff, W.D.6
  • 46
    • 0346850583 scopus 로고    scopus 로고
    • Lack of negative charge in the E46Q mutant of photoactive yellow protein prevents partial unfolding of the blue-shifted intermediate
    • Derix, N. M., R. W. Wechselberger, M. A. van der Horst, K. J. Hellingwerf, R. Boelens, R. Kaptein, and N. A. van Nuland. 2003. Lack of negative charge in the E46Q mutant of photoactive yellow protein prevents partial unfolding of the blue-shifted intermediate. Biochemistry. 42:14501-14506.
    • (2003) Biochemistry , vol.42 , pp. 14501-14506
    • Derix, N.M.1    Wechselberger, R.W.2    van der Horst, M.A.3    Hellingwerf, K.J.4    Boelens, R.5    Kaptein, R.6    van Nuland, N.A.7
  • 47
    • 0031808074 scopus 로고    scopus 로고
    • A helix propensity scale based on experimental studies of peptides and proteins
    • Pace, C. N., and J. M. Scholtz. 1998. A helix propensity scale based on experimental studies of peptides and proteins. Biophys. J. 75:422-427.
    • (1998) Biophys. J , vol.75 , pp. 422-427
    • Pace, C.N.1    Scholtz, J.M.2
  • 51
    • 0032544202 scopus 로고    scopus 로고
    • New insights into the photocycle of Ectothiorhodospira halophila photoactive yellow protein: Photorecovery of the long-lived photobleached intermediate in the Met100Ala mutant
    • Devanathan, S., U. K. Genick, I. L. Canestrelli, T. E. Meyer, M. A. Cusanovich, E. D. Getzoff, and G. Tollin. 1998. New insights into the photocycle of Ectothiorhodospira halophila photoactive yellow protein: photorecovery of the long-lived photobleached intermediate in the Met100Ala mutant. Biochemistry. 37:11563-11568.
    • (1998) Biochemistry , vol.37 , pp. 11563-11568
    • Devanathan, S.1    Genick, U.K.2    Canestrelli, I.L.3    Meyer, T.E.4    Cusanovich, M.A.5    Getzoff, E.D.6    Tollin, G.7


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