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Volumn 16, Issue 11, 2007, Pages 2350-2359

Engineering and rapid selection of a low-affinity glucose/galactose-binding protein for a glucose biosensor

Author keywords

Focused library; GGBP; Glucose galactose binding protein; Low affinity; Screening; Structure based site saturation mutagenesis

Indexed keywords

ARGININE; GALAPTIN; GLUCOSE;

EID: 35648996014     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.073119507     Document Type: Article
Times cited : (38)

References (42)
  • 1
    • 35648931080 scopus 로고    scopus 로고
    • Amiss, T.J., Nycz, C.M., Pitner, J.B., Sherman, D.B., and Wright, D.J. 2003. Binding protein as biosensors. U.S. Patent Application July 17, 2003/0134346A1. http://www.freepatentsonline.com/20030134346.html.
    • Amiss, T.J., Nycz, C.M., Pitner, J.B., Sherman, D.B., and Wright, D.J. 2003. Binding protein as biosensors. U.S. Patent Application July 17, 2003/0134346A1. http://www.freepatentsonline.com/20030134346.html.
  • 2
    • 35648946461 scopus 로고    scopus 로고
    • Amiss, T.J., Pitner, J.B., Freitas, T.C., and Giel, J.L. 2005. Compositions and methods for measuring analyte concentrations. U.S. Patent Application May 26, 2005/0112685A1. http://www.freepatentsonline.com/ 20050112685.html.
    • Amiss, T.J., Pitner, J.B., Freitas, T.C., and Giel, J.L. 2005. Compositions and methods for measuring analyte concentrations. U.S. Patent Application May 26, 2005/0112685A1. http://www.freepatentsonline.com/ 20050112685.html.
  • 3
    • 35648962034 scopus 로고    scopus 로고
    • Amiss, T., Snowden, E., and Pitner, J.B. 2006. Methods of screening proteins. U.S. Patent Application Febuary 23, 2006/0040327A1. http://www.freepatentsonline.com/20060040327.html.
    • Amiss, T., Snowden, E., and Pitner, J.B. 2006. Methods of screening proteins. U.S. Patent Application Febuary 23, 2006/0040327A1. http://www.freepatentsonline.com/20060040327.html.
  • 6
    • 0015217104 scopus 로고
    • Transport properties of the galactose-binding protein of Escherichia coli. Occurrence of two conformational states
    • Boos, W. and Gordon, A.S. 1971. Transport properties of the galactose-binding protein of Escherichia coli. Occurrence of two conformational states. J. Biol. Chem. 246: 621-628.
    • (1971) J. Biol. Chem , vol.246 , pp. 621-628
    • Boos, W.1    Gordon, A.S.2
  • 7
    • 0015500285 scopus 로고
    • Transport properties of the galactose-binding protein of Escherichia coli. Substrate-induced conformational change
    • Boos, W., Gordon, A.S., Hall, R.E., and Price, H.D. 1972. Transport properties of the galactose-binding protein of Escherichia coli. Substrate-induced conformational change. J. Biol. Chem. 247: 917-924.
    • (1972) J. Biol. Chem , vol.247 , pp. 917-924
    • Boos, W.1    Gordon, A.S.2    Hall, R.E.3    Price, H.D.4
  • 8
    • 34249781722 scopus 로고    scopus 로고
    • Conformational changes of glucose/galactose-binding protein illuminated by open unliganded, and ultra-high-resolution ligand-bound structures
    • doi: 10.1110/ps.062707807
    • Borrok, M.J., Kiessling, L.L., and Forest, K.T. 2007. Conformational changes of glucose/galactose-binding protein illuminated by open unliganded, and ultra-high-resolution ligand-bound structures. Protein Sci. 16: 1032-1041. doi: 10.1110/ps.062707807.
    • (2007) Protein Sci , vol.16 , pp. 1032-1041
    • Borrok, M.J.1    Kiessling, L.L.2    Forest, K.T.3
  • 10
    • 0035014528 scopus 로고    scopus 로고
    • Isolation of high-affinity ligand-binding proteins by periplasmic expression with cytometric screening (PECS)
    • Chen, G., Hayhurst, A., Thomas, J.G., Harvey, B.R., Iverson, B.L., and Georgiou, G. 2001. Isolation of high-affinity ligand-binding proteins by periplasmic expression with cytometric screening (PECS). Nat. Biotechnol. 19: 537-542.
    • (2001) Nat. Biotechnol , vol.19 , pp. 537-542
    • Chen, G.1    Hayhurst, A.2    Thomas, J.G.3    Harvey, B.R.4    Iverson, B.L.5    Georgiou, G.6
  • 11
    • 17644419994 scopus 로고    scopus 로고
    • Directed evolution of specific receptor-ligand pairs for use in the creation of gene switches
    • Chockalingam, K., Chen, Z., Katzenellenbogen, J.A., and Zhao, H. 2005. Directed evolution of specific receptor-ligand pairs for use in the creation of gene switches. Proc. Natl. Acad. Sci. 102: 5691-5696.
    • (2005) Proc. Natl. Acad. Sci , vol.102 , pp. 5691-5696
    • Chockalingam, K.1    Chen, Z.2    Katzenellenbogen, J.A.3    Zhao, H.4
  • 12
    • 0024403619 scopus 로고
    • High-resolution mapping of hGH-receptor interactions by alanine-scanning mutagenesis
    • Cunningham, B.C. and Wells, J.A. 1989. High-resolution mapping of hGH-receptor interactions by alanine-scanning mutagenesis. Science 244: 1081-1085.
    • (1989) Science , vol.244 , pp. 1081-1085
    • Cunningham, B.C.1    Wells, J.A.2
  • 13
    • 0347992016 scopus 로고    scopus 로고
    • Amelioration of the cost of conjugative plasmid carriage in Eschericha coli K12
    • Dahlberg, C. and Chao, L. 2003. Amelioration of the cost of conjugative plasmid carriage in Eschericha coli K12. Genetics 165: 1641-1649.
    • (2003) Genetics , vol.165 , pp. 1641-1649
    • Dahlberg, C.1    Chao, L.2
  • 15
    • 24344451972 scopus 로고    scopus 로고
    • Construction and optimization of a family of genetically encoded metabolite sensors by semirational protein engineering
    • Deuschle, K., Okumoto, S., Fehr, M., Looger, L.L., Kozhukh, L., and Frommer, W.B. 2005. Construction and optimization of a family of genetically encoded metabolite sensors by semirational protein engineering. Protein Sci. 14: 2304-2314.
    • (2005) Protein Sci , vol.14 , pp. 2304-2314
    • Deuschle, K.1    Okumoto, S.2    Fehr, M.3    Looger, L.L.4    Kozhukh, L.5    Frommer, W.B.6
  • 16
    • 20544449855 scopus 로고    scopus 로고
    • Why high-error-rate random mutagenesis libraries are enriched in functional and improved proteins
    • Drummond, D.A., Iverson, B.L., Georgiou, G., and Arnold, F.H. 2005. Why high-error-rate random mutagenesis libraries are enriched in functional and improved proteins. J. Mol. Biol. 350: 806-816.
    • (2005) J. Mol. Biol , vol.350 , pp. 806-816
    • Drummond, D.A.1    Iverson, B.L.2    Georgiou, G.3    Arnold, F.H.4
  • 17
    • 35648946460 scopus 로고    scopus 로고
    • Ellington, A. and Cherry, J.M. 1997. Characteristics of amino acids. In Current protocols in molecular biology (eds. F.M. Ausubel et al.). pp. A.1C.1-A.1C.12. John Wiley, New York.
    • Ellington, A. and Cherry, J.M. 1997. Characteristics of amino acids. In Current protocols in molecular biology (eds. F.M. Ausubel et al.). pp. A.1C.1-A.1C.12. John Wiley, New York.
  • 18
    • 0042926892 scopus 로고    scopus 로고
    • Phage display as a tool for the directed evolution of enzymes
    • Fernandez-Gacio, A., Uguen, M., and Fastrez, J. 2003. Phage display as a tool for the directed evolution of enzymes. Trends Biotechnol. 21: 408-414.
    • (2003) Trends Biotechnol , vol.21 , pp. 408-414
    • Fernandez-Gacio, A.1    Uguen, M.2    Fastrez, J.3
  • 19
    • 0032054156 scopus 로고    scopus 로고
    • Protein engineering and the development of generic biosensors
    • Hellinga, H.W. and Marvin, J.S. 1998. Protein engineering and the development of generic biosensors. Trends Biotechnol. 16: 183-189.
    • (1998) Trends Biotechnol , vol.16 , pp. 183-189
    • Hellinga, H.W.1    Marvin, J.S.2
  • 20
    • 0036841628 scopus 로고    scopus 로고
    • Creating randomized amino acid libraries with the QuikChange Multi Site-Directed Mutagenesis Kit
    • 1162
    • Hogrefe, H.H., Cline, J., Youngblood, G.L., and Allen, R.M. 2002. Creating randomized amino acid libraries with the QuikChange Multi Site-Directed Mutagenesis Kit. Biotechniques 33: 1158-1160, 1162, 1164-1165.
    • (2002) Biotechniques , vol.33
    • Hogrefe, H.H.1    Cline, J.2    Youngblood, G.L.3    Allen, R.M.4
  • 21
    • 27144431943 scopus 로고    scopus 로고
    • Selecting and screening recombinant antibody libraries
    • Hoogenboom, H.R. 2005. Selecting and screening recombinant antibody libraries. Nat. Biotechnol. 23: 1105-1116.
    • (2005) Nat. Biotechnol , vol.23 , pp. 1105-1116
    • Hoogenboom, H.R.1
  • 22
    • 0346725085 scopus 로고    scopus 로고
    • Direct detection of glucose by surface plasmon resonance with bacterial glucose/galactose-binding protein
    • Hsieh, H.V., Pfeiffer, Z.A., Amiss, T.J., Sherman, D.B., and Pitner, J.B. 2004. Direct detection of glucose by surface plasmon resonance with bacterial glucose/galactose-binding protein. Biosens. Bioelectron. 19: 653-660.
    • (2004) Biosens. Bioelectron , vol.19 , pp. 653-660
    • Hsieh, H.V.1    Pfeiffer, Z.A.2    Amiss, T.J.3    Sherman, D.B.4    Pitner, J.B.5
  • 24
    • 3543106035 scopus 로고    scopus 로고
    • Novel methods for directed evolution of enzymes: Quality not quantity
    • Lutz, S. and Patrick, W.M. 2004. Novel methods for directed evolution of enzymes: Quality not quantity. Curr. Opin. Biotechnol. 15: 291-297.
    • (2004) Curr. Opin. Biotechnol , vol.15 , pp. 291-297
    • Lutz, S.1    Patrick, W.M.2
  • 25
    • 0034863015 scopus 로고    scopus 로고
    • Manipulation of ligand binding affinity by exploitation of conformational coupling
    • Marvin, J.S. and Hellinga, H.W. 2001. Manipulation of ligand binding affinity by exploitation of conformational coupling. Nat. Struct. Biol. 8: 795-798.
    • (2001) Nat. Struct. Biol , vol.8 , pp. 795-798
    • Marvin, J.S.1    Hellinga, H.W.2
  • 26
    • 34249680261 scopus 로고    scopus 로고
    • Isolation of engineered, full-length antibodies from libraries expressed in Escherichia coli
    • Mazor, Y., Blarcom, T.V., Mabry, R., Iverson, B.L., and Georgiou, G. 2007. Isolation of engineered, full-length antibodies from libraries expressed in Escherichia coli. Nat. Biotechnol. 25: 563-565.
    • (2007) Nat. Biotechnol , vol.25 , pp. 563-565
    • Mazor, Y.1    Blarcom, T.V.2    Mabry, R.3    Iverson, B.L.4    Georgiou, G.5
  • 27
    • 0021062151 scopus 로고
    • Rates of ligand binding to periplasmic proteins involved in bacterial transport and chemotaxis
    • Miller III, D.M., Olson, J.S., Pflugrath, J.W., and Quiocho, F.A. 1983. Rates of ligand binding to periplasmic proteins involved in bacterial transport and chemotaxis. J. Biol. Chem. 258: 13665-13672.
    • (1983) J. Biol. Chem , vol.258 , pp. 13665-13672
    • Miller III, D.M.1    Olson, J.S.2    Pflugrath, J.W.3    Quiocho, F.A.4
  • 28
    • 0033904795 scopus 로고    scopus 로고
    • High-throughput screening of enzyme libraries
    • Olsen, M., Iverson, B., and Georgiou, G. 2000. High-throughput screening of enzyme libraries. Curr. Opin. Biotechnol. 11: 331-337.
    • (2000) Curr. Opin. Biotechnol , vol.11 , pp. 331-337
    • Olsen, M.1    Iverson, B.2    Georgiou, G.3
  • 29
    • 24044554219 scopus 로고    scopus 로고
    • Site-saturation mutagenesis is more efficient than DNA shuffling for the directed evolution of β-fucosidase from β-galactosidase
    • Parikh, M.R. and Matsumura, I. 2005. Site-saturation mutagenesis is more efficient than DNA shuffling for the directed evolution of β-fucosidase from β-galactosidase. J. Mol. Biol. 352: 621-628.
    • (2005) J. Mol. Biol , vol.352 , pp. 621-628
    • Parikh, M.R.1    Matsumura, I.2
  • 30
    • 0025054642 scopus 로고
    • Binding of a monoclonal antibody and its Fab fragment to supported phospholipid monolayers measured by total internal reflection fluorescence microscopy
    • Pisarchick, M.L. and Thompson, N.L. 1990. Binding of a monoclonal antibody and its Fab fragment to supported phospholipid monolayers measured by total internal reflection fluorescence microscopy. Biophys. J. 58: 1235-1249.
    • (1990) Biophys. J , vol.58 , pp. 1235-1249
    • Pisarchick, M.L.1    Thompson, N.L.2
  • 31
    • 0029981539 scopus 로고    scopus 로고
    • Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: Variation of common themes
    • Quiocho, F.A. and Ledvina, P.S. 1996. Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: Variation of common themes. Mol. Microbiol. 20: 17-25.
    • (1996) Mol. Microbiol , vol.20 , pp. 17-25
    • Quiocho, F.A.1    Ledvina, P.S.2
  • 32
    • 34248567845 scopus 로고    scopus 로고
    • Iterative saturation mutagenesis (ISM) for rapid directed evolution of functional enzymes
    • doi: 10.1038/nprot.2007.72
    • Reetz, M.T. and Carballeira, J.D. 2007. Iterative saturation mutagenesis (ISM) for rapid directed evolution of functional enzymes. Nat. Protoc. 2: 891-903. doi: 10.1038/nprot.2007.72.
    • (2007) Nat. Protoc , vol.2 , pp. 891-903
    • Reetz, M.T.1    Carballeira, J.D.2
  • 33
    • 0036177713 scopus 로고    scopus 로고
    • Guidelines and recommendations for laboratory analysis in the diagnosis and management of Diabetes Mellitus
    • Sacks, D.B., Bruns, D.E., Goldstein, D.E., Maclaren, N.K., McDonald, J.M., and Parrott, M. 2002. Guidelines and recommendations for laboratory analysis in the diagnosis and management of Diabetes Mellitus. Clin. Chem. 48: 436-472.
    • (2002) Clin. Chem , vol.48 , pp. 436-472
    • Sacks, D.B.1    Bruns, D.E.2    Goldstein, D.E.3    Maclaren, N.K.4    McDonald, J.M.5    Parrott, M.6
  • 34
    • 0035399396 scopus 로고    scopus 로고
    • A novel reagentless sensing system for measuring glucose based on the galactose/glucose-binding protein
    • Salins, L.L., Ware, R.A., Ensor, C.M., and Daunert, S. 2001. A novel reagentless sensing system for measuring glucose based on the galactose/glucose-binding protein. Anal. Biochem. 294: 19-26.
    • (2001) Anal. Biochem , vol.294 , pp. 19-26
    • Salins, L.L.1    Ware, R.A.2    Ensor, C.M.3    Daunert, S.4
  • 36
    • 0023256886 scopus 로고
    • A novel calcium binding site in the galactose-binding protein of bacterial transport and chemotaxis
    • Vyas, N.K., Vyas, M.N., and Quiocho, F.A. 1987. A novel calcium binding site in the galactose-binding protein of bacterial transport and chemotaxis. Nature 327: 635-638.
    • (1987) Nature , vol.327 , pp. 635-638
    • Vyas, N.K.1    Vyas, M.N.2    Quiocho, F.A.3
  • 37
    • 0024237631 scopus 로고
    • Sugar and signal-transducer binding sites of the Escherichia coli galactose chemoreceptor protein
    • Vyas, N.K., Vyas, M.N., and Quiocho, F.A. 1988. Sugar and signal-transducer binding sites of the Escherichia coli galactose chemoreceptor protein. Science 242: 1290-1295.
    • (1988) Science , vol.242 , pp. 1290-1295
    • Vyas, N.K.1    Vyas, M.N.2    Quiocho, F.A.3
  • 38
    • 0028244277 scopus 로고
    • Crystallographic analysis of the epimeric and anomeric specificity of the periplasmic transport/chemosensory protein receptor for D-glucose and D-galactose
    • Vyas, M.N., Vyas, N.K., and Quiocho, F.A. 1994. Crystallographic analysis of the epimeric and anomeric specificity of the periplasmic transport/chemosensory protein receptor for D-glucose and D-galactose. Biochemistry 33: 4762-4768.
    • (1994) Biochemistry , vol.33 , pp. 4762-4768
    • Vyas, M.N.1    Vyas, N.K.2    Quiocho, F.A.3
  • 39
    • 0242501562 scopus 로고    scopus 로고
    • Genetic engineering of an allosterically based glucose indicator protein for continuous glucose monitoring by fluorescence resonance energy transfer
    • Ye, K. and Schultz, J.S. 2003. Genetic engineering of an allosterically based glucose indicator protein for continuous glucose monitoring by fluorescence resonance energy transfer. Anal. Chem. 75: 3451-3459.
    • (2003) Anal. Chem , vol.75 , pp. 3451-3459
    • Ye, K.1    Schultz, J.S.2
  • 41
    • 3843146246 scopus 로고    scopus 로고
    • An efficient one-step sitedirected and site-saturation mutagenesis protocol
    • doi: 10.1093/nar/gnh110
    • Zheng, L., Baumann, U., and Reymond, J.L. 2004. An efficient one-step sitedirected and site-saturation mutagenesis protocol. Nucleic Acids Res. 32: e115. doi: 10.1093/nar/gnh110.
    • (2004) Nucleic Acids Res , vol.32
    • Zheng, L.1    Baumann, U.2    Reymond, J.L.3
  • 42
    • 0025799559 scopus 로고    scopus 로고
    • Zhou, L.Q. and Cass, A.E.G. 1991. Periplasmic binding protein based biosensors. 1. Preliminary study of maltose binding protein as sensing element for maltose biosensor. Biosens. Bioelectron. 6: 445-450. Protein Science (2007), 16:2360-2367.
    • Zhou, L.Q. and Cass, A.E.G. 1991. Periplasmic binding protein based biosensors. 1. Preliminary study of maltose binding protein as sensing element for maltose biosensor. Biosens. Bioelectron. 6: 445-450. Protein Science (2007), 16:2360-2367.


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