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Genetic code reprograming and synthetic biology


Much of the success to understand the genetic code in the past two decades has stemmed from the development of experimental methods to introduce artificial coding rules in vivo. Suppression (or read-through) of the stop codon (commonly the amber codon TAG) by the orthogonal translation apparatus enables the genetic code expansion. The key engineered orthogonal components, aminoacyl-tRNA synthetase and the suppressor tRNA (RS/tRNA) pair, can be transiently introduced into living cells via DNA injection, transformation, transfection, electroporation and viral delivery.  The presence of the RS/tRNA allows the incorporation of an unnatural amino acid (Uaa) with unique properties such as light-sensitive, chemical-reactive into proteins in situ.


We will explore two research directions: 

1) To apply methods associated with the genetic code expansion to understand the structure-function relationship of proteins.  The site-specific incorporation of Uaas, with chemical and spectroscopic properties absent in the natural amino acids repertoire, has been proved to be very useful to correlate the functional changes arising from a single point mutation.

2) To investigate the possibility of building basic functional proteins with a minimal set of amino acid repertoire. This fundamental approach is driven by the interest in understanding the standard genetic code. Theoretical and bioinformatic investigations suggest that small set of amino acids in the genetic code bear the property to generate all major secondary structure motifs observed in proteins. Results in this field will also help clarifying current concepts and ideas about the origin and evolution of the genetic code.

Selected Publications