Chromophore aspartate oxidation-decarboxylation in the green-to-red conversion of a fluorescent protein from Zoanthus sp. 2

Biochemistry

Volumn 46, Issue 41, 2007, Pages 11528-11535

  Pakhomov, Alexey A ^a   Martynov, Vladimir I ^a  

^a SHEMYAKIN OVCHINNIKOV INSTITUTE OF BIOORGANIC CHEMISTRY   (Russian Federation)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CHROMOPHORES; FLUORESCENCE; MOLECULAR STRUCTURE; REACTION RATES; SUBSTITUTION REACTIONS;

CHROMOPHORE ASPARTATE; DECARBOXYLATION; FLUORESCENT PROTEINS; GREEN FLUORESCENT PROTEIN (GFP);

PROTEINS;

GREEN FLUORESCENT PROTEIN; OXOACID;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CHROMATOPHORE; DECARBOXYLATION; KINETICS; MARINE SPECIES; MASS SPECTROMETRY; MUTAGENESIS; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; ZOANTHUS;

ANIMALS; ASPARTIC ACID; DECARBOXYLATION; GREEN FLUORESCENT PROTEINS; LUMINESCENT PROTEINS; MASS SPECTROMETRY; MODELS, MOLECULAR; MUTAGENESIS; OXIDATION-REDUCTION; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SEA ANEMONES; SPECTROPHOTOMETRY;

CONDYLACTIS GIGANTEA; DENDRONEPHTHYA SP.; DISCOSOMA CORAL; ZOANTHUS; ZOANTHUS SP.;

EID: 35348917373     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700721x     Document Type: Article

References (23)

1. Giepmans, B. N., Adams, S. R., Ellisman, M. H., and Tsien, R. Y. (2006) The fluorescent toolbox for assessing protein location and function, Science 312, 217-224.
2. Chudakov, D. M., Lukyanov, S., and Lukyanov, K. A. (2005) Fluorescent proteins as a toolkit for in vivo imaging, Trends Biotechnol. 23, 605-613.
3. Gross, L. A., Baird, G. S., Hoffman, R. C., Baldridge, K. K., and Tsien, R. Y. (2000) The structure of the chromophore within DsRed, a red fluorescent protein from coral, Proc. Natl. Acad. Sci. U.S.A. 97, 11990-11995.
4. Wall, M. A., Socolich, M., and Ranganathan, R. (2000) The structural basis for red fluorescence in the tetrameric GFP homolog DsRed, Nat. Struct. Biol. 7, 1133-1138.
5. Yarbrough, D., Wachter, R. M., Kallio, K., Matz, M. V., and Remington, S. J. (2001) Refined crystal structure of DsRed, a red fluorescent protein from coral, at 2.0-Å resolution, Proc. Natl. Acad. Sci. U.S.A. 98, 462-467.
6. Petersen, J., Wilmann, P. G., Beddoe, T., Oakley, A. J., Devenish, R. J., Prescott, M., and Rossjohn, J. (2003) The 2.0-Å crystal structure of eqFP611, a far red fluorescent protein from the sea anemone Entacmaea quadricolor, J. Biol. Chem. 278, 44626-44631.
7. Prescott, M., Ling, M., Beddoe, T., Oakley, A. J., Dove, S., Hoegh-Guldberg, O., Devenish, R. J., and Rossjohn, J. (2003) The 2.2 Å crystal structure of a pocilloporin pigment reveals a nonplanar chromophore conformation, Structure 11, 275-284.
8. Martynov, V. I., Maksimov, B. I., Martynova, N. Y., Pakhomov, A. A., Gurskaya, N. G., and Lukyanov, S. A. (2003) A purple-blue chromoprotein from Goniopora tenuidens belongs to the DsRed subfamily of GFP-like proteins, J. Biol. Chem. 278, 46288-46292.
9. Pakhomov, A. A., Pletneva, N. V., Balashova, T. A., and Martynov, V. I. (2006) Structure and reactivity of the chromophore of a GFP-like chromoprotein from Condylactis gigantea, Biochemistry 45, 7256-7264.
10. Labas, Y. A., Gurskaya, N. G., Yanushevich, Y. G., Fradkov, A. F., Lukyanov, K. A., Lukyanov, S. A., and Matz, M. V. (2002) Diversity and evolution of the green fluorescent protein family, Proc. Natl. Acad. Sci. U.S.A. 99, 4256-4261.
11. Pletneva, N., Pletnev, S., Tikhonova, T., Popov, V., Martynov, V., and Pletnev, V. (2006) Structure of a red fluorescent protein from Zoanthus, zRFP574, reveals a novel chromophore, Acta Crystallogr. D62, 527-532.
12. Gill, S. C., and von Hippel, P. H. (1989) Calculation of protein extinction coefficients from amino acid sequence data, Anal. Biochem. 182, 319-326.
13. Burmeister, W. P. (2000) Structural changes in a cryo-cooled protein crystal owing to radiation damage, Acta Crystallogr. D56, 328-341.
14. van Thor, J. J., Gensch, T., Hellingwerf, K. J., and Johnson, L. N. (2002) Phototransformation of green fluorescent protein with UV and visible light leads to decarboxylation of glutamate 222, Nat. Struct. Biol. 9, 37-41.
15. Pakhomov, A. A., Martynova, N. Y., Gurskaya, N. G., Balashova, T. A., and Martynov, V. I. (2004) Photoconversion of the chromophore of a fluorescent protein from Dendronephthya sp., Biochemistry (Moscow, Russ. Fed.) 69, 901-908.
16. Hoops, S., Sahle, S., Gauges, R., Lee, C., Pahle, J., Simus, N., Singhal, M., Xu, L., Mendes, P., and Kummer, U. (2006) COPASI: A COmplex PAthway Simulator, Bioinformatics 22, 3067-3074.
17. Verkhusha, V. V., Chudakov, D. M., Gurskaya, N. G., Lukyanov, S., and Lukyanov, K. A. (2004) Common pathway for the red chromophore formation in fluorescent proteins and chromoproteins, Chem. Biol. 11, 845-854.
18. Chan, M. C., Karasawa, S., Mizuno, H., Bosanac, I., Ho, D., Privé, G. G., Miyawaki, A., and Ikura, M. (2006) Structural characterization of a blue chromoprotein and its yellow mutant from the sea anemone Cnidopus japonicus, J. Biol. Chem. 281, 37813-37819.
19. Remington, S. J., Wachter, R. M., Yarbrough, D. K., Branchaud, B., Anderson, D. C., Kallio, K., and Lukyanov, K. A. (2005) zFP538, a yellow-fluorescent protein from Zoanthus, contains a novel three-ring chromophore, Biochemistry 44, 202-212.
20. Highbarger, L. A., Gerlt, J. A., and Kenyon, G. L. (1996) Mechanism of the reaction catalyzed by acetoacetate decarboxylase. Importance of lysine 116 in determining the pKa of active-site lysine 115, Biochemistry 35, 41-46.
21. Liu, D., Hwang, C. C., and Cook, P. F. (2002) Alternative substrates for malic enzyme: Oxidative decarboxylation of L-aspartate, Biochemistry 41, 12200-12203.
22. Begley, T. P., and Ealick, S. E. (2004) Enzymatic reactions involving novel mechanisms of carbanion stabilization, Curr. Opin. Chem. Biol. 8, 508-515.
23. Terskikh, A., Fradkov, A., Ermakova, G., Zaraisky, A., Tan, P., Kajava, A. V., Zhao, X., Lukyanov, S., Matz, M., Kim, S., Weissman, I., and Sieben, P. (2000) "Fluorescent timer": Protein that changes color with time, Science 290, 1585-1588.