Directed Evolution in Protein Functionality Improvement

단백질 기능 향상을 위한 방향적 진화

  • 강환구 (한남대학교 화학공학과 생물화공실험실) ;
  • 김학성 (한국과학기술원 생물과학과 생물화학공학 연구실)
  • Published : 2001.04.01

Abstract

The dynamic evolution process has resulted in the myriad shapes, functions, and systems evident in every living organism. For centuries, people have been harnessing the power of evolution to produce new varieties of plants and animals, such as producing tomatoes from berries and Chihuahuas from wolves. Now scientists are using it to produce better molecules, ranging from drugs to industrial chemicals, and doing it in days or weeks rather than eons. The ingenious process, which creates genetic diversity and selects those with desired features in the laboratory, is called directed evolution or test tube evolution. In this paper, concepts of directed molecular evolution and some examples will be discussed.

Keywords

References

  1. v.3 no.6 Mutagenic PCR. PCR Methods Appl Cadwell, R. C.;G. F. Joyce
  2. Science v.229 no.4710 A general method for saturation mutagenesis of cloned DNA fragments Myers, R. M.;L. S. Lerman;T. Maniatis
  3. Methods Mol Biol v.57 An efficient random mutagenesis technique using an E. coli mutator strain Greener, A.;M. Callahan;B. Jerpseth
  4. Proc Natl Acad Sci U S A v.93 no.8 Creation of drug-specific herpes simplex virus type 1 thymidine kinase mutants for genetherapy. Black, M. E. et. al.
  5. Protein Eng. v.6 no.3 Recursive ensemble mutagenesis. Delagrave, S.;E. R. Goldman;D. C. Youvan
  6. Proc Natl Acad Sci U S A v.91 no.22 DNA shuffling by random fragmenttion and reassembly: in vitro recombination for molecular evolution Stemmer, W. P.
  7. Nature v.370 no.6488 Rapid evolution of a protein in vitro by DNA shuffling Stemmer, W. P.
  8. Nature v.391 no.6664 DNA shuffling of a family of genes from diverse species accelerates directed evolution Crameri, A.(et al)
  9. Nat Biotechnol v.17 no.8 Evolution of a cytokine using DNA family shuffling Chang, C. C.(et al)
  10. Design by directed evolution. Acct. Chem. Res. v.31 no.3 Arnold, F. H.
  11. Proc Natl Acad Sci U S A v.94 no.9 Directed evolution of a fucosidase from a galactosidase by DNA shuffling and screening. Zhang, J. H.;G. Dawes;W. P. Stemmer
  12. Protein Eng v.12 no.1 Directed evolution converts subtilisin E into a functional equivalent of thermitase Zhao, H.;F. H. Arnold
  13. J. Biochem v.126 no.5 Directed evolution of thermostable kanamycin-resistance gene: a convenient selection marker for Thermus thermophilus Hoseki, J. (et al.)
  14. Nat Biotechnol v.18 no.3 Inverting enantioselectivity by directed evolution of hydantoinase for improved production of L-methionine May, O.;P. T. Nguyen;F. H. Arnold
  15. Curr Opin Chem Biol v.3 no.1 Directed evolution of biocatalysts. Arnold, F. H.;A. A. Volkov
  16. Curr Opin Chem Biol v.2 no.3 Combinatorial protein design by in vitro recombination Giver, L.;F. H. Arnold
  17. Biotechnol Bioeng v.69 no.5 Characterization of Trichoderma reesei cellobiohydrolase Cel7A secreted from Pichia pastoris using two different promoters Boer, H.;T. T. Teeri;A. Koivula
  18. Nat Biotechnol v.17 no.7 Directed evolution of the surface chemistry of the reporter enzyme beta-glucuronidase Matsumura, I. (et al)
  19. Proc Natl Acad Sci U S A v.90 no.12 Tuning the activity of an enzyme for unusual environments: Sequential random mutagenesis of subtilisin E for catalysis in dimethylformamide Chen, K.;F. H. Arnold
  20. Science v.261 no.5123 Genetic algorithms: Principles of natural selection applied to computation Forrest, S.
  21. Manual of Industrial Microbiology and Biotechnology(2nd Ed.) Method for optimizing industrial enzymes by directed evolution Zhao, H. (et al.);A. L. Demain;J. E. Davies(Eds.)
  22. Nucleic Acids Res v.25 no.6 Optimization of DNA shuffling for high fidelity recombination Zhao, H.;F. H. Arnold
  23. Proc Natl Acad Sci U S A v.94 no.15 Functional and nonfunctional mutations distinguished by random recombination of homologous genes Zhao, H.;F. H. Arnold
  24. Eur J Biochem v.148 no.2 Studies of the cellulolytic system of Trichoderma reesei QM 9414. Reaction specificity and thermodynamics of interactions of small substrates and ligands with the 1,4-beta-glucan cellobiohydrolase Ⅱ van Tilbeurgh, H. (et al.)
  25. Nature Biotechnology v.19 Coco W. M. (et al.)