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Volumn 121, Issue 5, 1997, Pages 876-880

Functional expression and site-directed mutagenesis of photoactive yellow T protein

Author keywords

Chromophore protein interaction; Expression; In vitro mutagenesis; Opsin shift; Photoactive yellow protein

Indexed keywords

BACTERIAL PROTEIN; MUTANT PROTEIN;

EID: 0030914406     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021668     Document Type: Article
Times cited : (119)

References (21)
  • 1
    • 0022430790 scopus 로고
    • Isolation and characterization of soluble cytochromes, ferredoxins and other chromophoric proteins from the halophilic phototrophic bacterium Ectothiorhodospira halophila
    • Meyer, T.E. (1985) Isolation and characterization of soluble cytochromes, ferredoxins and other chromophoric proteins from the halophilic phototrophic bacterium Ectothiorhodospira halophila. Biochim. Biophys. Acta 806, 175-183
    • (1985) Biochim. Biophys. Acta , vol.806 , pp. 175-183
    • Meyer, T.E.1
  • 2
    • 0027324441 scopus 로고
    • The eubacterium Ectothiorhodospira halophila is negatively phototactic, with a wavelength dependence that fits the absorption spectrum of the photoactive yellow protein
    • Sprenger, W.W., Hoff, W.D., Armitage, J.P., and Hellingwerf, K.J. (1993) The eubacterium Ectothiorhodospira halophila is negatively phototactic, with a wavelength dependence that fits the absorption spectrum of the photoactive yellow protein. J. Bacteriol. 175, 3096-3104
    • (1993) J. Bacteriol. , vol.175 , pp. 3096-3104
    • Sprenger, W.W.1    Hoff, W.D.2    Armitage, J.P.3    Hellingwerf, K.J.4
  • 3
    • 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., Yakali, E., Cusanovich, M.A., and Tollin, G. (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
  • 4
    • 84989696264 scopus 로고
    • Low temperature absorbance and fluorescence spectroscopy of the photoactive yellow protein from Ectothiorhodospira halophila
    • Hoff, W.D., Kwa, S.L.S., Van Grondelle, R., and Hellingwerf, K.J. (1992) Low temperature absorbance and fluorescence spectroscopy of the photoactive yellow protein from Ectothiorhodospira halophila. Photochem. Photobiol. 56, 529-539
    • (1992) Photochem. Photobiol. , vol.56 , pp. 529-539
    • Hoff, W.D.1    Kwa, S.L.S.2    Van Grondelle, R.3    Hellingwerf, K.J.4
  • 6
    • 0029803844 scopus 로고    scopus 로고
    • Photoreaction cycle of photoactive yellow protein from Ectothiorhodospira halophila studied by low-temperature spectroscopy
    • Imamoto, Y., Kataoka, M., and Tokunaga, F. (1996) Photoreaction cycle of photoactive yellow protein from Ectothiorhodospira halophila studied by low-temperature spectroscopy. Biochemistry 35, 14047-14053
    • (1996) Biochemistry , vol.35 , pp. 14047-14053
    • Imamoto, Y.1    Kataoka, M.2    Tokunaga, F.3
  • 7
    • 0029964634 scopus 로고    scopus 로고
    • Evidence for trans-cis isomerization of the p-coumaric acid chromophore as the photochemical basis of the photocycle of photoactive yellow protein
    • Kort, R., Vonk, H., Xu, X., Hoff, W.D., Crielaard, W., and Hellingwerf, K.J. (1996) Evidence for trans-cis isomerization of the p-coumaric acid chromophore as the photochemical basis of the photocycle of photoactive yellow protein. FEBS Lett. 382, 73-78
    • (1996) FEBS Lett. , vol.382 , pp. 73-78
    • Kort, R.1    Vonk, H.2    Xu, X.3    Hoff, W.D.4    Crielaard, W.5    Hellingwerf, K.J.6
  • 8
    • 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., Devreese, B.V., Van Bun, S.M., Hoff, W.D., Hellingwerf, K.J., Meyer, T.E., McRee, D.E., and Cusanovich, M.A. (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
  • 9
    • 0028577744 scopus 로고
    • Complete chemical structure of photoactive yellow protein: Novel thioester-linked 4-hydroxycinnamyl chromophore and photocycle chemistry
    • Baca, M., Borgstahl, G.E.O., Boissinot, M., Burke, P.M., Williams, D.R., Slater, K.A., and Getzoff, E.D. (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.O.2    Boissinot, M.3    Burke, P.M.4    Williams, D.R.5    Slater, K.A.6    Getzoff, E.D.7
  • 10
    • 0029110488 scopus 로고
    • 1.4 A structure of photoactive yellow protein, a cytosolic photoreceptor: Unusual fold, active site, and chromophore
    • Borgstahl, G.E.O., Williams, D.R., and Getzoff, E.D. (1995) 1.4 A 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.O.1    Williams, D.R.2    Getzoff, E.D.3
  • 12
    • 0028832513 scopus 로고
    • Resonance Raman evidence that the thioester-linked 4-hydroxycinnamyl chromophore of photoactive yellow protein is deprotonated
    • Kim, M., Mathies, R.A., Hoff, W.D., and Hellingwerf, K.J. (1995) Resonance Raman evidence that the thioester-linked 4-hydroxycinnamyl 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
  • 13
    • 0028868422 scopus 로고
    • Reconstitution photoactive yellow protein from apoprotein and p-coumaric acid derivatives
    • Imamoto, Y., Ito, T., Kataoka, M., and Tokunaga, F. (1995) Reconstitution 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
  • 15
    • 0027960310 scopus 로고
    • Phylogenetic relationships among vertebrate visual pigments
    • Hisatomi, O., Kayada, S., Aoki, Y., Iwasa, T., and Tokunaga, F. (1994) Phylogenetic relationships among vertebrate visual pigments. Vision Res. 34, 3097-3102
    • (1994) Vision Res. , vol.34 , pp. 3097-3102
    • Hisatomi, O.1    Kayada, S.2    Aoki, Y.3    Iwasa, T.4    Tokunaga, F.5
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0029892214 scopus 로고    scopus 로고
    • Sequence evidence for strong conservation of the photoactive yellow proteins from the halophilic phototrophic bacteria Chromatium salexigens and Rhodospirillum salexigens
    • Koh, M., Van Driessche, G., Samyn, B., Hoff, W.D., Meyer, T.E., Cusanovich, M.A., and Van Beeumen, J.J. (1996) Sequence evidence for strong conservation of the photoactive yellow proteins from the halophilic phototrophic bacteria Chromatium salexigens and Rhodospirillum 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
  • 18
    • 0028318245 scopus 로고
    • The photoactive yellow protein from Ectothiorhodospira halophila as studied with a highly specific polyclonal antiserum: (intra) cellular localization, regulation of expression, and taxonomic distribution of cross-reacting proteins
    • Hoff, W.D., Sprenger, W.W., Postma, P.W., Meyer, T.E., Veenhuis, M., Leguijt, T., and Hellingwerf, K.J. (1994) The photoactive yellow protein from Ectothiorhodospira halophila as studied with a highly specific polyclonal antiserum: (intra) cellular localization, regulation of expression, and taxonomic distribution of cross-reacting proteins. J. Bacteriol. 176, 3920-3927
    • (1994) J. Bacteriol. , vol.176 , pp. 3920-3927
    • Hoff, W.D.1    Sprenger, W.W.2    Postma, P.W.3    Meyer, T.E.4    Veenhuis, M.5    Leguijt, T.6    Hellingwerf, K.J.7
  • 20
    • 0024024413 scopus 로고
    • Aspartic acid substitutions affect proton translocation by bacteriorhodopsin
    • Mogi, T., Stern, L.J., Marti, T., Chao, B.H., and Khorana, H.G. (1988) Aspartic acid substitutions affect proton translocation by bacteriorhodopsin. Proc. Natl. Acad. Sci. USA 85, 4148-4152
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 4148-4152
    • Mogi, T.1    Stern, L.J.2    Marti, T.3    Chao, B.H.4    Khorana, H.G.5
  • 21
    • 0030446427 scopus 로고    scopus 로고
    • Glu46 donates a proton to the 4-hydroxycinnamate anion chromophore during the photocycle of photoactive yellow protein
    • Xie, A., Hoff, W.D., Kroon, A.R., and Hellingwerf, K.J. (1996) Glu46 donates a proton to the 4-hydroxycinnamate anion chromophore during the photocycle of photoactive yellow protein. Biochemistry 35, 14671-14678
    • (1996) Biochemistry , vol.35 , pp. 14671-14678
    • Xie, A.1    Hoff, W.D.2    Kroon, A.R.3    Hellingwerf, K.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.