메뉴 건너뛰기




Volumn 44, Issue 49, 2005, Pages 16211-16220

Defining the role of arginine 96 in green fluorescent protein fluorophore biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; BIOSYNTHESIS; CHROMOPHORES; CONFORMATIONS; CRYSTALLOGRAPHY; FLUORESCENCE; MOLECULAR BIOLOGY;

EID: 28944445805     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051388j     Document Type: Article
Times cited : (67)

References (42)
  • 1
    • 0032607587 scopus 로고    scopus 로고
    • Understanding structure-function relationships in the Aequorea victoria green fluorescent protein
    • Cubitt, A. B., Woollenweber, L. A., and Heim, R. (1999) Understanding structure-function relationships in the Aequorea victoria green fluorescent protein, Methods Cell Biol. 58, 19-30.
    • (1999) Methods Cell Biol. , vol.58 , pp. 19-30
    • Cubitt, A.B.1    Woollenweber, L.A.2    Heim, R.3
  • 2
    • 0029847806 scopus 로고    scopus 로고
    • Crystal structure of the Aequorea victoria green fluorescent protein
    • Ormo, M., Cubitt, A. B., Kallio, K., Gross, L. A., Tsien, R. Y., and Remington, S. J. (1996) Crystal structure of the Aequorea victoria green fluorescent protein, Science 273, 1392-5.
    • (1996) Science , vol.273 , pp. 1392-1395
    • Ormo, M.1    Cubitt, A.B.2    Kallio, K.3    Gross, L.A.4    Tsien, R.Y.5    Remington, S.J.6
  • 3
    • 0028580734 scopus 로고
    • Wavelength mutations and posttranslational autoxidation of green fluorescent protein
    • Heim, R., Prasher, D. C., and Tsien, R. Y. (1994) Wavelength mutations and posttranslational autoxidation of green fluorescent protein, Proc. Natl Acad. Sci. U.S.A. 91, 12501-4.
    • (1994) Proc. Natl Acad. Sci. U.S.A. , vol.91 , pp. 12501-12504
    • Heim, R.1    Prasher, D.C.2    Tsien, R.Y.3
  • 4
    • 0029780351 scopus 로고    scopus 로고
    • The molecular structure of green fluorescent protein
    • Yang, F., Moss, L. G., and Phillips, G. N., Jr. (1996) The molecular structure of green fluorescent protein, Nat. Biotechnol. 14, 1246-51.
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1246-1251
    • Yang, F.1    Moss, L.G.2    Phillips Jr., G.N.3
  • 5
    • 0032516480 scopus 로고    scopus 로고
    • pH-dependent fluorescence of a heterologously expressed Aequorea green fluorescent protein mutant: In situ spectral characteristics and applicability to intracellular pH estimation
    • Robey, R. B., Ruiz, O., Santos, A. V., Ma, J., Kear, F., Wang, L. J., Li, C. J., Bernardo, A. A., and Arruda, J. A. (1998) pH-dependent fluorescence of a heterologously expressed Aequorea green fluorescent protein mutant: In situ spectral characteristics and applicability to intracellular pH estimation, Biochemistry 37, 9894-901.
    • (1998) Biochemistry , vol.37 , pp. 9894-9901
    • Robey, R.B.1    Ruiz, O.2    Santos, A.V.3    Ma, J.4    Kear, F.5    Wang, L.J.6    Li, C.J.7    Bernardo, A.A.8    Arruda, J.A.9
  • 6
    • 0031885535 scopus 로고    scopus 로고
    • Green fluorescent protein as a noninvasive intracellular pH indicator
    • Kneen, M., Farinas, J., Li, Y., and Verkman, A. S. (1998) Green fluorescent protein as a noninvasive intracellular pH indicator, Biophys. J. 74, 1591-9.
    • (1998) Biophys. J. , vol.74 , pp. 1591-1599
    • Kneen, M.1    Farinas, J.2    Li, Y.3    Verkman, A.S.4
  • 7
    • 0029147089 scopus 로고
    • Green fluorescent protein as a reporter of gene expression and protein localization
    • Kain, S. R., Adams, M., Kondepudi, A., Yang, T. T., Ward, W. W., and Kitts, P. (1995) Green fluorescent protein as a reporter of gene expression and protein localization, BioTechniques 19, 650-5.
    • (1995) BioTechniques , vol.19 , pp. 650-655
    • Kain, S.R.1    Adams, M.2    Kondepudi, A.3    Yang, T.T.4    Ward, W.W.5    Kitts, P.6
  • 8
  • 9
    • 0033609034 scopus 로고    scopus 로고
    • Structural and spectral response of green fluorescent protein variants to changes in pH
    • Elsliger, M. A., Wachter, R. M., Hanson, G. T., Kallio, K., and Remington, S. J. (1999) Structural and spectral response of green fluorescent protein variants to changes in pH, Biochemistry 38, 5296-301.
    • (1999) Biochemistry , vol.38 , pp. 5296-5301
    • Elsliger, M.A.1    Wachter, R.M.2    Hanson, G.T.3    Kallio, K.4    Remington, S.J.5
  • 10
    • 0041154057 scopus 로고    scopus 로고
    • Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile
    • Schwede, T. F., Retey, J., and Schulz, G. E. (1999) Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile, Biochemistry 38, 5355-61.
    • (1999) Biochemistry , vol.38 , pp. 5355-5361
    • Schwede, T.F.1    Retey, J.2    Schulz, G.E.3
  • 11
    • 0035478435 scopus 로고    scopus 로고
    • Methylidene-imidazolone: A novel electrophile for substrate activation
    • Poppe, L. (2001) Methylidene-imidazolone: A novel electrophile for substrate activation, Curr. Opin. Chem. Biol. 5, 512-24.
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 512-524
    • Poppe, L.1
  • 12
    • 4444306767 scopus 로고    scopus 로고
    • Crystal structure of phenylalanine ammonia lyase: Multiple helix dipoles implicated in catalysis
    • Calabrese, J. C., Jordan, D. B., Boodhoo, A., Sariaslani, S., and Vannelli, T. (2004) Crystal structure of phenylalanine ammonia lyase: Multiple helix dipoles implicated in catalysis, Biochemistry 43, 11403-16.
    • (2004) Biochemistry , vol.43 , pp. 11403-11416
    • Calabrese, J.C.1    Jordan, D.B.2    Boodhoo, A.3    Sariaslani, S.4    Vannelli, T.5
  • 13
    • 0035808253 scopus 로고    scopus 로고
    • Mutants of Discosoma red fluorescent protein with a GFP-like chromophore
    • Wiehler, J., von Hummel, J., and Steipe, B. (2001) Mutants of Discosoma red fluorescent protein with a GFP-like chromophore, FEBS Lett. 487, 384-9.
    • (2001) FEBS Lett. , vol.487 , pp. 384-389
    • Wiehler, J.1    Von Hummel, J.2    Steipe, B.3
  • 14
    • 0034710921 scopus 로고    scopus 로고
    • The structure of the chromophore within DsRed, a red fluorescent protein from coral, Proc
    • 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, 11990-5.
    • (2000) Natl. Acad. Sci. U.S.A. , vol.97 , pp. 11990-11995
    • Gross, L.A.1    Baird, G.S.2    Hoffman, R.C.3    Baldridge, K.K.4    Tsien, R.Y.5
  • 15
    • 0242666241 scopus 로고    scopus 로고
    • The 2.0-Å crystal structure of eqFP611, a far red fluorescent protein from the sea anemone Entacmaea quadricolor
    • 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, 44626-31.
    • (2003) J. Biol. Chem. , vol.278 , pp. 44626-44631
    • Petersen, J.1    Wilmann, P.G.2    Beddoe, T.3    Oakley, A.J.4    Devenish, R.J.5    Prescott, M.6    Rossjohn, J.7
  • 16
    • 0242361312 scopus 로고    scopus 로고
    • Photoinduced peptide cleavage in the green-to-red conversion of a fluorescent protein
    • Mizuno, H., Mal, T. K., Tong, K. I., Ando, R., Furuta, T., Ikura, M., and Miyawaki, A. (2003) Photoinduced peptide cleavage in the green-to-red conversion of a fluorescent protein, Mol. Cell 12, 1051-8.
    • (2003) Mol. Cell , vol.12 , pp. 1051-1058
    • Mizuno, H.1    Mal, T.K.2    Tong, K.I.3    Ando, R.4    Furuta, T.5    Ikura, M.6    Miyawaki, A.7
  • 17
    • 6344289261 scopus 로고    scopus 로고
    • Traditional GFP-type cyclization and unexpected fragmentation site in a purple chromoprotein from Anemonia sulcata, asFP595
    • Zagranichny, V. E., Rudenko, N. V., Gorokhovatsky, A. Y., Zakharov, M. V., Balashova, T. A., and Arseniev, A. S. (2004) Traditional GFP-type cyclization and unexpected fragmentation site in a purple chromoprotein from Anemonia sulcata, asFP595, Biochemistry 43, 13598-603.
    • (2004) Biochemistry , vol.43 , pp. 13598-13603
    • Zagranichny, V.E.1    Rudenko, N.V.2    Gorokhovatsky, A.Y.3    Zakharov, M.V.4    Balashova, T.A.5    Arseniev, A.S.6
  • 18
    • 11144267737 scopus 로고    scopus 로고
    • Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein
    • Shaner, N. C., Campbell, R. E., Steinbach, P. A., Giepmans, B. N., Palmer, A. E., and Tsien, R. Y. (2004) Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein, Nat. Biotechnol. 22, 1567-72.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1567-1572
    • Shaner, N.C.1    Campbell, R.E.2    Steinbach, P.A.3    Giepmans, B.N.4    Palmer, A.E.5    Tsien, R.Y.6
  • 20
    • 0029994339 scopus 로고    scopus 로고
    • Enhanced green fluorescence by the expression of an Aequorea victoria green fluorescent protein mutant in mono- And dicotyledonous plant cells
    • Reichel, C., Mathur, J., Eckes, P., Langenkemper, K., Koncz, C., Schell, J., Reiss, B., and Maas, C. (1996) Enhanced green fluorescence by the expression of an Aequorea victoria green fluorescent protein mutant in mono- and dicotyledonous plant cells, Proc. Natl. Acad. Sci. U.S.A. 93, 5888-93.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 5888-5893
    • Reichel, C.1    Mathur, J.2    Eckes, P.3    Langenkemper, K.4    Koncz, C.5    Schell, J.6    Reiss, B.7    Maas, C.8
  • 21
    • 0032532156 scopus 로고    scopus 로고
    • Structural basis of spectral shifts in the yellow-emission variants of green fluorescent protein
    • Wachter, R. M., Elsliger, M. A., Kallio, K., Hanson, G. T., and Remington, S. J. (1998) Structural basis of spectral shifts in the yellow-emission variants of green fluorescent protein, Structure 6, 1267-77.
    • (1998) Structure , vol.6 , pp. 1267-1277
    • Wachter, R.M.1    Elsliger, M.A.2    Kallio, K.3    Hanson, G.T.4    Remington, S.J.5
  • 22
    • 0142027791 scopus 로고    scopus 로고
    • Mechanism and energetics of green fluorescent protein chromophore synthesis revealed by trapped intermediate structures
    • Barondeau, D. P., Putnam, C. D., Kassmann, C. J., Tainer, J. A., and Getzoff, E. D. (2003) Mechanism and energetics of green fluorescent protein chromophore synthesis revealed by trapped intermediate structures, Proc. Natl. Acad. Sci. U.S.A. 100, 12111-6.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 12111-12116
    • Barondeau, D.P.1    Putnam, C.D.2    Kassmann, C.J.3    Tainer, J.A.4    Getzoff, E.D.5
  • 23
    • 0032515404 scopus 로고    scopus 로고
    • A computational analysis of the unique protein induced tight turn that results in posttranslational chromophore formation in green fluorescent protein
    • Branchini, B. R., Nemser, A. R., and Zimmer, M. (1998) A computational analysis of the unique protein induced tight turn that results in posttranslational chromophore formation in green fluorescent protein, J. Am. Chem. Soc. 120, 1-6.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 1-6
    • Branchini, B.R.1    Nemser, A.R.2    Zimmer, M.3
  • 24
    • 0028921834 scopus 로고
    • Improved green fluorescence
    • Heim, R., Cubitt, A. B., and Tsien, R. Y. (1995) Improved green fluorescence, Nature 373, 663-4.
    • (1995) Nature , vol.373 , pp. 663-664
    • Heim, R.1    Cubitt, A.B.2    Tsien, R.Y.3
  • 25
    • 13544256284 scopus 로고    scopus 로고
    • Understanding GFP Chromophore Biosynthesis: Controlling Backbone Cyclization and Modifying Post-translational Chemistry
    • Barondeau, D. P., Kassmann, C. J., Tainer, J. A., and Getzoff, E. D. (2005) Understanding GFP Chromophore Biosynthesis: Controlling Backbone Cyclization and Modifying Post-translational Chemistry, Biochemistry 44, 1960-70.
    • (2005) Biochemistry , vol.44 , pp. 1960-1970
    • Barondeau, D.P.1    Kassmann, C.J.2    Tainer, J.A.3    Getzoff, E.D.4
  • 26
    • 0031006611 scopus 로고    scopus 로고
    • Chromophore formation in green fluorescent protein
    • Reid, B. G., and Flynn, G. C. (1997) Chromophore formation in green fluorescent protein, Biochemistry 36, 6786-91.
    • (1997) Biochemistry , vol.36 , pp. 6786-6791
    • Reid, B.G.1    Flynn, G.C.2
  • 27
    • 0029347056 scopus 로고
    • Rapid purification of recombinant green fluorescent protein using the hydrophobic properties of an HPLC size-exclusion column
    • Deschamps, J. R., Miller, C. E., and Ward, K. B. (1995) Rapid purification of recombinant green fluorescent protein using the hydrophobic properties of an HPLC size-exclusion column, Protein Expression Purif. 6, 555-8.
    • (1995) Protein Expression Purif. , vol.6 , pp. 555-558
    • Deschamps, J.R.1    Miller, C.E.2    Ward, K.B.3
  • 28
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray Diffraction Data Collected in Oscillation Mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray Diffraction Data Collected in Oscillation Mode, Methods Enzymol. 276, 307-26.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 29
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for Protein Crystallography
    • Collaborative Computational Project, No. 4 (1994) The CCP4 Suite: Programs for Protein Crystallography, Acta Crystallogr. D50, 760-3.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 30
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit: A versatile program for manipulating atomic coordinates and electron density
    • McRee, D. E. (1999) XtalView/Xfit: A versatile program for manipulating atomic coordinates and electron density, J. Struct. Biol. 125, 156-65.
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 32
    • 0030880598 scopus 로고    scopus 로고
    • SHELXL: High-resolution refinement
    • Sheldrick, G. M., and Schneider, T. R. (1997) SHELXL: High-resolution refinement, Methods Enzymol. 277, 319-43.
    • (1997) Methods Enzymol. , vol.277 , pp. 319-343
    • Sheldrick, G.M.1    Schneider, T.R.2
  • 34
    • 0029670330 scopus 로고    scopus 로고
    • Improved green fluorescent protein by molecular evolution using DNA shuffling
    • Crameri, A., Whitehorn, E. A., Tate, E., and Stemmer, W. P. (1996) Improved green fluorescent protein by molecular evolution using DNA shuffling, Nat. Biotechnol. 14, 315-9.
    • (1996) Nat. Biotechnol. , vol.14 , pp. 315-319
    • Crameri, A.1    Whitehorn, E.A.2    Tate, E.3    Stemmer, W.P.4
  • 35
    • 0029973636 scopus 로고    scopus 로고
    • FACS-optimized mutants of the green fluorescentprotein (GFP)
    • Cormack, B. P., Valdivia, R. H., and Falkow, S. (1996) FACS-optimized mutants of the green fluorescentprotein (GFP), Gene 173, 33-8.
    • (1996) Gene , vol.173 , pp. 33-38
    • Cormack, B.P.1    Valdivia, R.H.2    Falkow, S.3
  • 36
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien, R. Y. (1998) The green fluorescent protein, Annu. Rev. Biochem. 67, 509-44.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 37
    • 0030087710 scopus 로고    scopus 로고
    • Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer
    • Heim, R., and Tsien, R. Y. (1996) Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer, Curr. Biol. 6, 178-82.
    • (1996) Curr. Biol. , vol.6 , pp. 178-182
    • Heim, R.1    Tsien, R.Y.2
  • 38
    • 0034604399 scopus 로고    scopus 로고
    • Crystallographic and energetic analysis of binding of selected anions to the yellow variants of green fluorescent protein
    • Wachter, R. M., Yarbrough, D., Kallio, K., and Remington, S. J. (2000) Crystallographic and energetic analysis of binding of selected anions to the yellow variants of green fluorescent protein, J. Mol. Biol. 301, 157-71.
    • (2000) J. Mol. Biol. , vol.301 , pp. 157-171
    • Wachter, R.M.1    Yarbrough, D.2    Kallio, K.3    Remington, S.J.4
  • 39
    • 0035152671 scopus 로고    scopus 로고
    • Theoretical study of the mechanism of peptide ring formation in green fluorescent protein
    • Siegbahn, P. E. M., Wirstam, M., and Zimmer, M. (2001) Theoretical study of the mechanism of peptide ring formation in green fluorescent protein, Int. J. Quantum Chem. 81, 169-86.
    • (2001) Int. J. Quantum Chem. , vol.81 , pp. 169-186
    • Siegbahn, P.E.M.1    Wirstam, M.2    Zimmer, M.3
  • 40
    • 0037137223 scopus 로고    scopus 로고
    • Binding of dioxygen to nonmetal sites in proteins: Exploration of the importance of binding site size versus hydrophobicity in the copper amine oxidase from Hansenula polymorpha
    • Goto, Y., and Klinman, J. P. (2002) Binding of dioxygen to nonmetal sites in proteins: Exploration of the importance of binding site size versus hydrophobicity in the copper amine oxidase from Hansenula polymorpha, Biochemistry 41, 13637-43.
    • (2002) Biochemistry , vol.41 , pp. 13637-13643
    • Goto, Y.1    Klinman, J.P.2
  • 41
    • 19744378582 scopus 로고    scopus 로고
    • Maturation efficiency, trypsin sensitivity, and optical properties of Arg96, Glu222, and Gly67 variants of green fluorescent protein
    • Sniegowski, J. A., Phail, M. E., and Wachter, R. M. (2005) Maturation efficiency, trypsin sensitivity, and optical properties of Arg96, Glu222, and Gly67 variants of green fluorescent protein, Biochem. Biophys. Res. Commun. 332, 657-63.
    • (2005) Biochem. Biophys. Res. Commun. , vol.332 , pp. 657-663
    • Sniegowski, J.A.1    Phail, M.E.2    Wachter, R.M.3
  • 42
    • 22544460277 scopus 로고    scopus 로고
    • Base catalysis of chromophore formation in Arg96 and Glu222 variants of green fluorescent protein
    • Sniegowski, J. A., Lappe, J. W., Patel, H. N., Huffman, H. A., and Wachter, R. M. (2005) Base catalysis of chromophore formation in Arg96 and Glu222 variants of green fluorescent protein, J. Biol. Chem. 280, 26248-55.
    • (2005) J. Biol. Chem. , vol.280 , pp. 26248-26255
    • Sniegowski, J.A.1    Lappe, J.W.2    Patel, H.N.3    Huffman, H.A.4    Wachter, R.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.