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Volumn 17, Issue 3, 1999, Pages 259-264

Directed evolution of thymidine kinase for AZT phosphorylation using DNA family shuffling

Author keywords

Gene transfer; Random mutagenesis; Sexual PCR DNA shuffling; Suicide gene; Zidovudine

Indexed keywords

DNA; THYMIDINE KINASE; ZIDOVUDINE;

EID: 0033037012     PISSN: 10870156     EISSN: None     Source Type: Journal    
DOI: 10.1038/7003     Document Type: Article
Times cited : (117)

References (33)
  • 1
    • 0028110130 scopus 로고
    • DNA shuffling by random fragmentation and reassembly: In vitro recombination for molecular evolution
    • Stemmer, W.P.C. DNA shuffling by random fragmentation and reassembly: in vitro recombination for molecular Evolution. Proc. Natl. Acad. Sci. USA 91, 10747-10751 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10747-10751
    • Stemmer, W.P.C.1
  • 2
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer, W.P.C. Rapid evolution of a protein in vitro by DNA shuffling. Nature 370, 389-391 (1994).
    • (1994) Nature , vol.370 , pp. 389-391
    • Stemmer, W.P.C.1
  • 3
    • 0030989062 scopus 로고    scopus 로고
    • Directed evolution of a fucosidase from a galactosidase by DNA shuffling and screening
    • Zhang, J.-H., Dawes, G. & Stemmer, W.P.C. Directed evolution of a fucosidase from a galactosidase by DNA shuffling and screening. Proc. Natl. Acad. Sci. USA 94, 4504-4509 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4504-4509
    • Zhang, J.-H.1    Dawes, G.2    Stemmer, W.P.C.3
  • 4
    • 0029670330 scopus 로고    scopus 로고
    • Improved green fluorescent protein by molecular evolution using DNA shuffling
    • Crameri, A.. Whitehorn, E.A., Tate, E. & Stemmer, W.P.C. Improved green fluorescent protein by molecular evolution using DNA shuffling. Nat. Biotechnol. 14, 315-319 (1996).
    • (1996) Nat. Biotechnol. , vol.14 , pp. 315-319
    • Crameri, A.1    Whitehorn, E.A.2    Tate, E.3    Stemmer, W.P.C.4
  • 5
    • 0031874849 scopus 로고    scopus 로고
    • Improved properties of FLP recombinase evolved by cycling mutagenesis
    • Buchholz, F., Angrand, P.-O. & Stewart, A.F. Improved properties of FLP recombinase evolved by cycling mutagenesis. Nat. Biotechnol. 16, 657-662 (1998).
    • (1998) Nat. Biotechnol. , vol.16 , pp. 657-662
    • Buchholz, F.1    Angrand, P.-O.2    Stewart, A.F.3
  • 6
    • 0032518266 scopus 로고    scopus 로고
    • DNA shuffling of a family of genes from diverse species accelerates directed evolution
    • Crameri, A., Raillard, S.-A., Bermudez. E. & Stemmer, W.P.C. DNA shuffling of a family of genes from diverse species accelerates directed evolution. Nature 391, 288-291 (1998).
    • (1998) Nature , vol.391 , pp. 288-291
    • Crameri, A.1    Raillard, S.-A.2    Bermudez, E.3    Stemmer, W.P.C.4
  • 7
    • 0031874757 scopus 로고    scopus 로고
    • Enhanced degradation of polychlorinated biphenyls by directed evolution of biphenyl dioxygenase
    • Kumamaru, T., Suenaga, H., Mitsuoka, M., Watanabe, T. & Furukawa, K. Enhanced degradation of polychlorinated biphenyls by directed evolution of biphenyl dioxygenase. Nat. Biotechnol. 16, 663-666 (1998).
    • (1998) Nat. Biotechnol. , vol.16 , pp. 663-666
    • Kumamaru, T.1    Suenaga, H.2    Mitsuoka, M.3    Watanabe, T.4    Furukawa, K.5
  • 8
    • 0003084227 scopus 로고    scopus 로고
    • eds. Fields, B.N., Knipe, D.M. & Howley, P.M. Lippincott-Raven, Philadelphia
    • Hirsch, M.S., Kaplan, J.C. & D'Aquila, R.T. in Fields virology (eds. Fields, B.N., Knipe, D.M. & Howley, P.M.) 431-466 (Lippincott-Raven, Philadelphia, 1996).
    • (1996) Fields Virology , pp. 431-466
    • Hirsch, M.S.1    Kaplan, J.C.2    D'Aquila, R.T.3
  • 10
    • 0343052856 scopus 로고    scopus 로고
    • Use of herpes simplex virus thymidine kinase to improve the antiviral activity of zidovudine
    • Guettari, N., Loubiere, L., Brisson, E. & Klatzmann, D. Use of herpes simplex virus thymidine kinase to improve the antiviral activity of zidovudine. Virology 235, 398-405 (1997).
    • (1997) Virology , vol.235 , pp. 398-405
    • Guettari, N.1    Loubiere, L.2    Brisson, E.3    Klatzmann, D.4
  • 11
    • 0030795311 scopus 로고    scopus 로고
    • Metabolism and activities of 3′-azido-2′,3′-dideoxythymidine and 2′,3′-didehydro-2′,3′-dideoxythymidine in herpesvirus thymidine kinase transduced T-lymphocytes
    • Drake, R.R. et al. Metabolism and activities of 3′-azido-2′,3′-dideoxythymidine and 2′,3′-didehydro-2′,3′-dideoxythymidine in herpesvirus thymidine kinase transduced T-lymphocytes. Antiviral Res. 35, 177-185 (1997).
    • (1997) Antiviral Res. , vol.35 , pp. 177-185
    • Drake, R.R.1
  • 12
    • 0026464790 scopus 로고
    • Viral thymidine kinases and their relatives
    • Gentry, G.A. Viral thymidine kinases and their relatives. Pharmacol. Ther. 54, 319-355 (1992).
    • (1992) Pharmacol. Ther. , vol.54 , pp. 319-355
    • Gentry, G.A.1
  • 13
    • 0027192014 scopus 로고
    • Thymidine kinase mutants obtained by random sequence selection
    • Munir, K.M., French, D.C. & Loeb, L.A. Thymidine kinase mutants obtained by random sequence selection. Proc. Natl. Acad. Sci. USA 90, 4012-4016 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4012-4016
    • Munir, K.M.1    French, D.C.2    Loeb, L.A.3
  • 14
    • 0027501570 scopus 로고
    • Identification of important residues within the putative nucleoside binding site of HSV-1 thymidine kinase by random sequence selection: Analysis of selected mutants in vitro
    • Black, M.E. & Loeb, L.A. Identification of important residues within the putative nucleoside binding site of HSV-1 thymidine kinase by random sequence selection: analysis of selected mutants in vitro. Biochemistry 32, 11618-11626 (1993).
    • (1993) Biochemistry , vol.32 , pp. 11618-11626
    • Black, M.E.1    Loeb, L.A.2
  • 15
    • 0029883624 scopus 로고    scopus 로고
    • Creation of drug-specific herpes simplex virus type 1 thymidine kinase mutants for gene therapy
    • Black, M.E., Newcomb, T.G., Wilson, H.-M.P. & Loeb, L.A. Creation of drug-specific herpes simplex virus type 1 thymidine kinase mutants for gene therapy. Proc. Natl. Acad. Sci. USA 93, 3525-3529 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3525-3529
    • Black, M.E.1    Newcomb, T.G.2    Wilson, H.-M.P.3    Loeb, L.A.4
  • 16
    • 0031587291 scopus 로고    scopus 로고
    • Strategies for the in vitro evolution of protein function: Enzyme evolution by random recombination of improved sequences
    • Moore, J.C., Jin, H.-M., Kuchner, O. & Arnold, F.H. Strategies for the in vitro evolution of protein function: enzyme evolution by random recombination of improved sequences. J. Mol. Biol. 273, 336-347 (1997).
    • (1997) J. Mol. Biol. , vol.273 , pp. 336-347
    • Moore, J.C.1    Jin, H.-M.2    Kuchner, O.3    Arnold, F.H.4
  • 17
    • 0030829025 scopus 로고    scopus 로고
    • The structures of thymidine kinase from Herpes simplex virus type 1 in complex with substrates and a substrate analog
    • Wild, K., Bohner, T., Folkers, G. & Schulz, G.E. The structures of thymidine kinase from Herpes simplex virus type 1 in complex with substrates and a substrate analog. Protein Sci. 6, 2097-2106 (1997).
    • (1997) Protein Sci. , vol.6 , pp. 2097-2106
    • Wild, K.1    Bohner, T.2    Folkers, G.3    Schulz, G.E.4
  • 18
    • 0029125949 scopus 로고
    • Crystal structures of the thymidine kinase from herpes simplex virus type-1 in complex with deoxythymidine and ganciclovir
    • 1995
    • Brown, D.G. et al. 1995. Crystal structures of the thymidine kinase from herpes simplex virus type-1 in complex with deoxythymidine and ganciclovir. Nat. Struct. Biol. 2, 876-881 (1995).
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 876-881
    • Brown, D.G.1
  • 19
    • 0032529367 scopus 로고    scopus 로고
    • Exploring the active site of herpes simplex virus type-1 thymidine kinase by x-ray crystallography of complexes with acyclovir and other ligands
    • Champness, J.N. et al. Exploring the active site of herpes simplex virus type-1 thymidine kinase by x-ray crystallography of complexes with acyclovir and other ligands. Struct. Funct. Genet. 32, 350-361 (1998).
    • (1998) Struct. Funct. Genet. , vol.32 , pp. 350-361
    • Champness, J.N.1
  • 20
    • 0032528262 scopus 로고    scopus 로고
    • Drug resistance of herpes simplex virus type 1: Structural considerations on the molecular level of the thymidine kinase
    • Kussmann-Gerber, S., Kuonen, O., Folkers, G., Pilger, B.D. & Scapozza, L. Drug resistance of herpes simplex virus type 1: structural considerations on the molecular level of the thymidine kinase. Eur. J. Biochem. 255, 472-481 (1998).
    • (1998) Eur. J. Biochem. , vol.255 , pp. 472-481
    • Kussmann-Gerber, S.1    Kuonen, O.2    Folkers, G.3    Pilger, B.D.4    Scapozza, L.5
  • 21
    • 0030845913 scopus 로고    scopus 로고
    • Structure of thymidylate kinase reveals the cause behind the limiting step in AZT activation
    • Lavie, A. et al. Structure of thymidylate kinase reveals the cause behind the limiting step in AZT activation. Nat. Struct. Biol. 4, 601-604 (1997).
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 601-604
    • Lavie, A.1
  • 22
    • 0030859182 scopus 로고    scopus 로고
    • The bottleneck in AZT activation
    • Lavie, A. et al. The bottleneck in AZT activation. Nat. Med. 3, 922-924 (1997).
    • (1997) Nat. Med. , vol.3 , pp. 922-924
    • Lavie, A.1
  • 23
    • 0031930544 scopus 로고    scopus 로고
    • Improving AZT efficacy
    • Balzarini, J. et al. Improving AZT efficacy. Nat. Med. 4, 132 (1998).
    • (1998) Nat. Med. , vol.4 , pp. 132
    • Balzarini, J.1
  • 24
    • 0031034761 scopus 로고    scopus 로고
    • Overexpression of DNA polymerase b sensitizes mammalian cells to 2′,3′-didexoycytidine and 3′-azido′-3′-deoxythymidine
    • Bouayadi, K. et al. Overexpression of DNA polymerase b sensitizes mammalian cells to 2′,3′-didexoycytidine and 3′-azido′-3′-deoxythymidine. Cancer Res. 57, 110-116 (1997).
    • (1997) Cancer Res. , vol.57 , pp. 110-116
    • Bouayadi, K.1
  • 25
    • 0030722164 scopus 로고    scopus 로고
    • Applications of DNA shuffling to pharmaceuticals and vaccines
    • Patten, P.A., Howard, R.J. & Stemmer, W.P.C. Applications of DNA shuffling to pharmaceuticals and vaccines. Curr. Opin. Biotechnol. 8, 724-733 (1997).
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 724-733
    • Patten, P.A.1    Howard, R.J.2    Stemmer, W.P.C.3
  • 26
    • 0014152202 scopus 로고
    • A deoxythymidine kinase deficient mutant of Escherichia coli. II. Mapping and transduction studies with phage phi 80
    • Igarashi, K., Hiraga, S. & Yura, T. A deoxythymidine kinase deficient mutant of Escherichia coli. II. Mapping and transduction studies with phage phi 80. Genetics 57, 643-654 (1967).
    • (1967) Genetics , vol.57 , pp. 643-654
    • Igarashi, K.1    Hiraga, S.2    Yura, T.3
  • 27
    • 0018735516 scopus 로고
    • Statistical analysis of enzyme data
    • Cleland, W.W. Statistical analysis of enzyme data. Methods Enzymol. 63, 103-138 (1979).
    • (1979) Methods Enzymol. , vol.63 , pp. 103-138
    • Cleland, W.W.1
  • 28
    • 0030741596 scopus 로고    scopus 로고
    • X-ray analysis of azido-thymidine diphosphate binding to nucleoside diphosphate kinase
    • Xu, Y. et al. X-ray analysis of azido-thymidine diphosphate binding to nucleoside diphosphate kinase. Proc. Natl. Acad. Sci. USA 94, 7162-7165 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7162-7165
    • Xu, Y.1
  • 29
    • 0029633186 scopus 로고
    • AMBER, A package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules
    • Perlman, D.A. et al. AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules. Comp. Phys. Commun. 91, 1-41 (1995).
    • (1995) Comp. Phys. Commun. , vol.91 , pp. 1-41
    • Perlman, D.A.1
  • 31
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moos, D.S. & Thornton, J.M.J. PROCHECK: a program to check the stereochemical quality of protein structures. Appl. Cryst. 26, 283-291 (1993).
    • (1993) Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moos, D.S.3    Thornton, J.M.J.4
  • 32
    • 0021871375 scopus 로고
    • A computational procedure for determining energetically favorable binding sites on biologically important macromolecules
    • Goodford, P.J. A computational procedure for determining energetically favorable binding sites on biologically important macromolecules. J. Med. Chem. 28, 849-857 (1985).
    • (1985) J. Med. Chem. , vol.28 , pp. 849-857
    • Goodford, P.J.1
  • 33
    • 0027439587 scopus 로고
    • Further development of hydrogen bond functions for use in determining energetically favorable binding sites on molecules of known structure
    • Wade, R.C. & Goodford, P.J. Further development of hydrogen bond functions for use in determining energetically favorable binding sites on molecules of known structure. J. Med. Chem. 36, 140-156 (1993).
    • (1993) J. Med. Chem. , vol.36 , pp. 140-156
    • Wade, R.C.1    Goodford, P.J.2


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