Prolegomena to future experimental efforts on genetic code engineering by expanding its amino acid repertoire

被引:200
作者
Budisa, N [1 ]
机构
[1] Max Planck Inst Biochem, Jr Res Grp Mol Biotechnol, D-82152 Martinsried, Germany
关键词
amino acids; biosynthesis; evolution; genetic code; proteins;
D O I
10.1002/anie.200300646
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Protein synthesis and its relation to the genetic code was for a long time a central issue in biology. Rapid experimental progress throughout the past decade, crowned with the recently elucidated ribosomal structures, provided an almost complete description of this process. In addition important experiments provided solid evidence that the natural protein translation machinery can be reprogrammed to encode genetically a vast number of non-coded (i.e. noncanonical) amino acids. Indeed, in the set of 20 canonical amino acids as prescribed by the universal genetic code, many desirable functionalities, such as halogeno, keto, cyano, azido, nitroso, nitro, and silyl groups, as well as C=C or C≡C bonds, are absent. The ability to encode genetically such chemical diversity will enable us to reprogram living cells, such as bacteria, to express tailor-made proteins exhibiting functional diversity. Accordingly, genetic code engineering has developed into an exciting emerging research field at the interface of biology, chemistry, and physics.
引用
收藏
页码:6426 / 6463
页数:38
相关论文
共 285 条
  • [21] Incorporation of an unnatural amino acid in the active site of porcine pancreatic phospholipase A(2). Substitution of histidine by 1,2,4-triazole-3-alanine yields an enzyme with high activity at acidic pH
    Beiboer, SHW
    vandenBerg, B
    Dekker, N
    Cox, RC
    Verheij, HM
    [J]. PROTEIN ENGINEERING, 1996, 9 (04): : 345 - 352
  • [22] Photoreactive bicyclic amino acids as substrates for mutant Escherichia coli phenylalanyl-tRNA synthetases
    Bentin, T
    Hamzavi, R
    Salomonsson, J
    Roy, H
    Ibba, M
    Nielsen, PE
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (19) : 19839 - 19845
  • [23] Orthogonal base pairs continue to evolve
    Bergstrom, DE
    [J]. CHEMISTRY & BIOLOGY, 2004, 11 (01): : 18 - 20
  • [24] Besse D, 1997, BIOL CHEM, V378, P211
  • [25] A tRNA aminoacylation system for non-natural amino acids based on a programmable ribozyme
    Bessho, Y
    Hodgson, DRW
    Suga, H
    [J]. NATURE BIOTECHNOLOGY, 2002, 20 (07) : 723 - 728
  • [26] SELENOCYSTEINE - THE 21ST AMINO-ACID
    BOCK, A
    FORCHHAMMER, K
    HEIDER, J
    LEINFELDER, W
    SAWERS, G
    VEPREK, B
    ZINONI, F
    [J]. MOLECULAR MICROBIOLOGY, 1991, 5 (03) : 515 - 520
  • [27] BOGOSIAN G, 1989, J BIOL CHEM, V264, P531
  • [28] BIO-INCORPORATION OF TELLUROMETHIONINE INTO BURIED RESIDUES OF DIHYDROFOLATE-REDUCTASE
    BOLES, JO
    LEWINSKI, K
    KUNKLE, M
    ODOM, JD
    DUNLAP, RB
    LEBIODA, L
    HATADA, M
    [J]. NATURE STRUCTURAL BIOLOGY, 1994, 1 (05): : 283 - 284
  • [29] Synthesis and incorporation of [6,7]-selenatryptophan into dihydrofolate reductase
    Boles, JO
    Henderson, J
    Hatch, D
    Silks, LA
    [J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2002, 298 (02) : 257 - 261
  • [30] PURIFICATION AND CHARACTERIZATION OF SELENOMETHIONYL THYMIDYLATE SYNTHASE FROM ESCHERICHIA-COLI - COMPARISON WITH THE WILD-TYPE ENZYME
    BOLES, JO
    CISNEROS, RJ
    WEIR, MS
    ODOM, JD
    VILLAFRANCA, JE
    DUNLAP, RB
    [J]. BIOCHEMISTRY, 1991, 30 (46) : 11073 - 11080