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Volumn 73, Issue 3, 2008, Pages 539-551

Understanding the role of Arg96 in structure and stability of green fluorescent protein

Author keywords

Chromophore structure; Circular dichroism; Conformational stability; Enhanced green fluorescent protein; Fluorescent protein; Green fluorescent protein; Point mutation

Indexed keywords

ACRYLAMIDE; ALANINE; ARGININE; CYSTEINE; ENHANCED GREEN FLUORESCENT PROTEIN; GLYCINE; GREEN FLUORESCENT PROTEIN; MUTANT PROTEIN; SERINE; TRYPTOPHAN;

EID: 57349182178     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22089     Document Type: Article
Times cited : (16)

References (57)
  • 2
    • 0029780351 scopus 로고    scopus 로고
    • The molecular structure of green fluorescent protein
    • Yang F, Moss LG, Phillips GN, Jr. The molecular structure of green fluorescent protein. Nat Biotechnol 1996;14:1246-1251.
    • (1996) Nat Biotechnol , vol.14 , pp. 1246-1251
    • Yang, F.1    Moss, L.G.2    Phillips Jr., G.N.3
  • 3
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien RY. The green fluorescent protein. Annu Rev Biochem 1998;67:509-544.
    • (1998) Annu Rev Biochem , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 4
    • 0032532156 scopus 로고    scopus 로고
    • Structural basis of spectral shifts in the yellow-emission variants of green fluorescent protein
    • Wachter RM, Elsliger MA, Kallio K, Hanson GT, Remington SJ. Structural basis of spectral shifts in the yellow-emission variants of green fluorescent protein. Structure 1998;6:1267-1277.
    • (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
  • 5
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics. J Mol Graph
    • Humphrey W, Dalke A, Schulten K. VMD: visual molecular dynamics. J Mol Graph 1996;14:33-38, 27-38.
    • (1996) , vol.14
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 6
    • 0028057108 scopus 로고    scopus 로고
    • Merritt EA, Murphy ME. Raster3D Version 2.0. A program for photorealistic molecular graphics. Acta Crystallogr D Biol Crystallogr 1994;50(Pt 6):869-873
    • Merritt EA, Murphy ME. Raster3D Version 2.0. A program for photorealistic molecular graphics. Acta Crystallogr D Biol Crystallogr 1994;50(Pt 6):869-873.
  • 7
    • 0017859622 scopus 로고
    • Chemical and physical properties of aequorin and the green fluorescent protein isolated from Aequorea forskalea
    • Prendergast FG, Mann KG. Chemical and physical properties of aequorin and the green fluorescent protein isolated from Aequorea forskalea. Biochemistry 1978;17:3448-3453.
    • (1978) Biochemistry , vol.17 , pp. 3448-3453
    • Prendergast, F.G.1    Mann, K.G.2
  • 9
    • 0027465627 scopus 로고
    • Chemical structure of the hexapeptide chromophore of the Aequorea green-fluorescent protein
    • Cody CW, Prasher DC, Westler WM, Prendergast FG, Ward WW. Chemical structure of the hexapeptide chromophore of the Aequorea green-fluorescent protein. Biochemistry 1993;32:1212-1218.
    • (1993) Biochemistry , vol.32 , pp. 1212-1218
    • Cody, C.W.1    Prasher, D.C.2    Westler, W.M.3    Prendergast, F.G.4    Ward, W.W.5
  • 10
    • 0029061274 scopus 로고
    • Green-fluorescent protein mutants with altered fluorescence excitation spectra
    • Ehrig T, O'Kane DJ, Prendergast FG. Green-fluorescent protein mutants with altered fluorescence excitation spectra. FEBS Lett 1995;367:163-166.
    • (1995) FEBS Lett , vol.367 , pp. 163-166
    • Ehrig, T.1    O'Kane, D.J.2    Prendergast, F.G.3
  • 11
    • 0031006611 scopus 로고    scopus 로고
    • Chromophore formation in green fluorescent protein
    • Reid BG, Flynn GC. Chromophore formation in green fluorescent protein. Biochemistry 1997;36:6786-6791.
    • (1997) Biochemistry , vol.36 , pp. 6786-6791
    • Reid, B.G.1    Flynn, G.C.2
  • 12
    • 0032621293 scopus 로고    scopus 로고
    • Biophysics of the green fluorescent protein
    • Prendergast FG. Biophysics of the green fluorescent protein. Methods Cell Biol 1999;58:1-18.
    • (1999) Methods Cell Biol , vol.58 , pp. 1-18
    • Prendergast, F.G.1
  • 13
    • 0019892005 scopus 로고
    • Renaturation of Aequorea green-fluorescent protein
    • Bokman SH, Ward WW. Renaturation of Aequorea green-fluorescent protein. Biochem Biophys Res Commun 1981;101:1372-1380.
    • (1981) Biochem Biophys Res Commun , vol.101 , pp. 1372-1380
    • Bokman, S.H.1    Ward, W.W.2
  • 14
    • 0020482348 scopus 로고
    • Reversible denaturation of Aequorea green-fluorescent protein: Physical separation and characterization of the renatured protein
    • Ward WW, Bokman SH. Reversible denaturation of Aequorea green-fluorescent protein: physical separation and characterization of the renatured protein. Biochemistry 1982;21:4535-4540.
    • (1982) Biochemistry , vol.21 , pp. 4535-4540
    • Ward, W.W.1    Bokman, S.H.2
  • 16
    • 0034601826 scopus 로고    scopus 로고
    • Folding of green fluorescent protein and the cycle3 mutant
    • Fukuda H, Arai M, Kuwajima K. Folding of green fluorescent protein and the cycle3 mutant. Biochemistry 2000;39:12025-12032.
    • (2000) Biochemistry , vol.39 , pp. 12025-12032
    • Fukuda, H.1    Arai, M.2    Kuwajima, K.3
  • 20
    • 0028921834 scopus 로고
    • Improved green fluorescence
    • Heim R, Cubitt AB, Tsien RY. Improved green fluorescence. Nature 1995;373:663-664.
    • (1995) Nature , vol.373 , pp. 663-664
    • Heim, R.1    Cubitt, A.B.2    Tsien, R.Y.3
  • 21
    • 0028580734 scopus 로고
    • Wavelength mutations and post-translational autoxidation of green fluorescent protein
    • Heim R, Prasher DC, Tsien RY. Wavelength mutations and post-translational autoxidation of green fluorescent protein. Proc Natl Acad Sci USA 1994;91:12501-12504.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12501-12504
    • Heim, R.1    Prasher, D.C.2    Tsien, R.Y.3
  • 22
    • 0032500053 scopus 로고    scopus 로고
    • Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins
    • Miesenbock G, De Angelis DA, Rothman JE. Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins. Nature 1998;394:192-195.
    • (1998) Nature , vol.394 , pp. 192-195
    • Miesenbock, G.1    De Angelis, D.A.2    Rothman, J.E.3
  • 23
    • 0034683125 scopus 로고    scopus 로고
    • Novel fluorescent protein from Discosoma coral and its mutants possesses a unique far-red fluorescence
    • Fradkov AF, Chen Y, Ding L, Barsova EV, Matz MV, Lukyanov SA. Novel fluorescent protein from Discosoma coral and its mutants possesses a unique far-red fluorescence. FEBS Lett 2000;479:127-130.
    • (2000) FEBS Lett , vol.479 , pp. 127-130
    • Fradkov, A.F.1    Chen, Y.2    Ding, L.3    Barsova, E.V.4    Matz, M.V.5    Lukyanov, S.A.6
  • 27
    • 0036138545 scopus 로고    scopus 로고
    • Rapidly maturing variants of the Discosoma red fluorescent protein (DsRed)
    • Bevis BJ, Glick BS. Rapidly maturing variants of the Discosoma red fluorescent protein (DsRed). Nat Biotechnol 2002;20:83-87.
    • (2002) Nat Biotechnol , vol.20 , pp. 83-87
    • Bevis, B.J.1    Glick, B.S.2
  • 28
    • 0035370120 scopus 로고    scopus 로고
    • Expression of fluorescently tagged connexins: A novel approach to rescue function of oligomeric DsRed-tagged proteins
    • Lauf U, Lopez P, Falk MM. Expression of fluorescently tagged connexins: a novel approach to rescue function of oligomeric DsRed-tagged proteins. FEBS Lett 2001;498:11-15.
    • (2001) FEBS Lett , vol.498 , pp. 11-15
    • Lauf, U.1    Lopez, P.2    Falk, M.M.3
  • 29
    • 0035839465 scopus 로고    scopus 로고
    • An enhanced mutant of red fluorescent protein DsRed for double labeling and developmental timer of neural fiber bundle formation
    • Verkhusha VV, Otsuna H, Awasaki T, Oda H, Tsukita S, Ito K. An enhanced mutant of red fluorescent protein DsRed for double labeling and developmental timer of neural fiber bundle formation. J Biol Chem 2001;276:29621-29624.
    • (2001) J Biol Chem , vol.276 , pp. 29621-29624
    • Verkhusha, V.V.1    Otsuna, H.2    Awasaki, T.3    Oda, H.4    Tsukita, S.5    Ito, K.6
  • 30
    • 0035957110 scopus 로고    scopus 로고
    • Red fluorescent protein from Discosoma as a fusion tag and a partner for fluorescence resonance energy transfer
    • Mizuno H, Sawano A, Eli P, Hama H, Miyawaki A. Red fluorescent protein from Discosoma as a fusion tag and a partner for fluorescence resonance energy transfer. Biochemistry 2001;40:2502-2510.
    • (2001) Biochemistry , vol.40 , pp. 2502-2510
    • Mizuno, H.1    Sawano, A.2    Eli, P.3    Hama, H.4    Miyawaki, A.5
  • 31
    • 0038758748 scopus 로고    scopus 로고
    • Measurements of the free luminal ER Ca(2+) concentration with targeted "cameleon" fluorescent proteins
    • Demaurex N, Frieden M. Measurements of the free luminal ER Ca(2+) concentration with targeted "cameleon" fluorescent proteins. Cell Calcium 2003;34:109-119.
    • (2003) Cell Calcium , vol.34 , pp. 109-119
    • Demaurex, N.1    Frieden, M.2
  • 34
    • 0141677840 scopus 로고    scopus 로고
    • A protein-chameleon: Conformational plasticity of alpha-synuclein, a disordered protein involved in neurodegenerative disorders
    • Uversky VN. A protein-chameleon: conformational plasticity of alpha-synuclein, a disordered protein involved in neurodegenerative disorders. J Biomol Struct Dyn 2003;21:211-234.
    • (2003) J Biomol Struct Dyn , vol.21 , pp. 211-234
    • Uversky, V.N.1
  • 35
    • 34548620297 scopus 로고    scopus 로고
    • Neuropathology, biochemistry, and biophysics of α-synuclein aggregation
    • Uversky VN. Neuropathology, biochemistry, and biophysics of α-synuclein aggregation. J Neurochem 2007;103:17-37.
    • (2007) J Neurochem , vol.103 , pp. 17-37
    • Uversky, V.N.1
  • 36
    • 33947713086 scopus 로고    scopus 로고
    • Photo-activity induced by amyloidogenesis
    • Tcherkasskaya O. Photo-activity induced by amyloidogenesis. Protein Sci 2007;16:561-571.
    • (2007) Protein Sci , vol.16 , pp. 561-571
    • Tcherkasskaya, O.1
  • 37
    • 22544460277 scopus 로고    scopus 로고
    • Base catalysis of chromophore formation in Arg96 and Glu222 variants of green fluorescent protein
    • Sniegowski JA, Lappe JW, Patel HN, Huffman HA, Wachter RM. Base catalysis of chromophore formation in Arg96 and Glu222 variants of green fluorescent protein. J Biol Chem 2005;280:26248-26255.
    • (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
  • 39
    • 19744378582 scopus 로고    scopus 로고
    • Maturation efficiency, trypsin sensitivity, and optical properties of Arg96, Glu222, and Gly67 variants of green fluorescent protein
    • Sniegowski JA, Phail ME, Wachter RM. Maturation efficiency, trypsin sensitivity, and optical properties of Arg96, Glu222, and Gly67 variants of green fluorescent protein. Biochem Biophys Res Commun 2005;332:657-663.
    • (2005) Biochem Biophys Res Commun , vol.332 , pp. 657-663
    • Sniegowski, J.A.1    Phail, M.E.2    Wachter, R.M.3
  • 40
    • 19744365121 scopus 로고    scopus 로고
    • The photophysics of green fluorescent protein: Influence of the key amino acids at positions 65, 203, and 222
    • Jung G, Wiehler J, Zumbusch A. The photophysics of green fluorescent protein: influence of the key amino acids at positions 65, 203, and 222. Biophys J 2005;88:1932-1947.
    • (2005) Biophys J , vol.88 , pp. 1932-1947
    • Jung, G.1    Wiehler, J.2    Zumbusch, A.3
  • 41
    • 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 BR, Nemser AR, Zimmer M. A computational analysis of the unique protein-induced tight turn that results in posttranslational chromophore formation in green fluorescent protein. J Am Chem Soc 1998;120:1-6.
    • (1998) J Am Chem Soc , vol.120 , pp. 1-6
    • Branchini, B.R.1    Nemser, A.R.2    Zimmer, M.3
  • 42
    • 85044704833 scopus 로고    scopus 로고
    • A complex of apparatus and programs for the measurement of spectral, polarization and kinetic characteristics of fluorescence in solution
    • Turoverov KK, Biktashev AG, Dorofeiuk AV, Kuznetsova IM. A complex of apparatus and programs for the measurement of spectral, polarization and kinetic characteristics of fluorescence in solution. Tsitologiia 1998;40:806-817.
    • (1998) Tsitologiia , vol.40 , pp. 806-817
    • Turoverov, K.K.1    Biktashev, A.G.2    Dorofeiuk, A.V.3    Kuznetsova, I.M.4
  • 43
    • 0000169232 scopus 로고
    • An algorithm for least-squares estimation of nonlinear parameters
    • Marquardt DW. An algorithm for least-squares estimation of nonlinear parameters. J Soc Indust Appl Math 1963;11:431-441.
    • (1963) J Soc Indust Appl Math , vol.11 , pp. 431-441
    • Marquardt, D.W.1
  • 46
    • 33746911626 scopus 로고    scopus 로고
    • The equilibrium unfolding intermediate observed at pH 4 and its relationship with the kinetic folding intermediates in green fluorescent protein
    • Enoki S, Maki K, Inobe T, Takahashi K, Kamagata K, Oroguchi T, Nakatani H, Tomoyori K, Kuwajima K. The equilibrium unfolding intermediate observed at pH 4 and its relationship with the kinetic folding intermediates in green fluorescent protein. J Mol Biol 2006;361:969-982.
    • (2006) J Mol Biol , vol.361 , pp. 969-982
    • Enoki, S.1    Maki, K.2    Inobe, T.3    Takahashi, K.4    Kamagata, K.5    Oroguchi, T.6    Nakatani, H.7    Tomoyori, K.8    Kuwajima, K.9
  • 47
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace CN. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol 1986;131:266-280.
    • (1986) Methods Enzymol , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 50
    • 34249657467 scopus 로고    scopus 로고
    • Stable intermediate states and high energy barriers in the unfolding of GFP
    • Huang JR, Craggs TD, Christodoulou J, Jackson SE. Stable intermediate states and high energy barriers in the unfolding of GFP. J Mol Biol 2007;370:356-371.
    • (2007) J Mol Biol , vol.370 , pp. 356-371
    • Huang, J.R.1    Craggs, T.D.2    Christodoulou, J.3    Jackson, S.E.4
  • 51
    • 0034053143 scopus 로고    scopus 로고
    • One- and twophoton excited fluorescence lifetimes and anisotropy decays of green fluorescent proteins
    • Volkmer A, Subramaniam V, Birch DJ, Jovin TM. One- and twophoton excited fluorescence lifetimes and anisotropy decays of green fluorescent proteins. Biophys J 2000;78:1589-1598.
    • (2000) Biophys J , vol.78 , pp. 1589-1598
    • Volkmer, A.1    Subramaniam, V.2    Birch, D.J.3    Jovin, T.M.4
  • 52
    • 34548816178 scopus 로고    scopus 로고
    • The rough energy landscape of superfolder GFP is linked to the chromophore
    • Andrews BT, Schoenfish AR, Roy M, Waldo G, Jennings PA. The rough energy landscape of superfolder GFP is linked to the chromophore. J Mol Biol 2007;373:476-490.
    • (2007) J Mol Biol , vol.373 , pp. 476-490
    • Andrews, B.T.1    Schoenfish, A.R.2    Roy, M.3    Waldo, G.4    Jennings, P.A.5
  • 55
    • 0037069399 scopus 로고    scopus 로고
    • Protein stabilization by urea and guanidine hydrochloride
    • Bhuyan AK. Protein stabilization by urea and guanidine hydrochloride. Biochemistry 2002;41:13386-13394.
    • (2002) Biochemistry , vol.41 , pp. 13386-13394
    • Bhuyan, A.K.1
  • 56
    • 0142027791 scopus 로고    scopus 로고
    • Mechanism and energetics of green fluorescent protein chromophore synthesis revealed by trapped intermediate structures
    • Barondeau DP, Putnam CD, Kassmann CJ, Tainer JA, Getzoff ED. Mechanism and energetics of green fluorescent protein chromophore synthesis revealed by trapped intermediate structures. Proc Natl Acad Sci USA 2003;100:12111-12116.
    • (2003) Proc Natl Acad Sci USA , 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
  • 57
    • 13544256284 scopus 로고    scopus 로고
    • Understanding GFP chromophore biosynthesis: Controlling backbone cyclization and modifying post-translational chemistry
    • Barondeau DP, Kassmann CJ, Tainer JA, Getzoff ED. Understanding GFP chromophore biosynthesis: controlling backbone cyclization and modifying post-translational chemistry. Biochemistry 2005;44:1960-1970.
    • (2005) Biochemistry , vol.44 , pp. 1960-1970
    • Barondeau, D.P.1    Kassmann, C.J.2    Tainer, J.A.3    Getzoff, E.D.4


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