Prolegomena to future experimental efforts on genetic code engineering by expanding its amino acid repertoire.
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[triple bond]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.
Budisa
Nediljko
N
Max-Planck-Institut für Biochemie, Junior Research Group "Moleculare Biotechnologie", Am Klopferspitz 18a, 82152 Martinsried bei München, Germany. budisa@biochem.mpg.de
D000596:Amino Acids / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D000818:Animals; D005815:Genetic Code / Q000235:genetics*; D005818:Genetic Engineering / Q000379:methods*; D006801:Humans; D014176:Protein Biosynthesis; D020543:Proteome / Q000235:genetics / Q000378:metabolism; D012270:Ribosomes / Q000235:genetics / Q000378:metabolism
D000596:Amino Acids; D020543:Proteome