Difference between revisions of "Team:Bielefeld-CeBiTec/Description"

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With their broad chemical and functional diversity ncAAs provide a variety of promising applications including proteinlabeling, photocaging, structure analysis and specific protein interactions. Therefore, the development of a new iGEM toolkit for the translational incorporation of non-canonical amino acids (ncAAs) in E. coli would be a great contribution to the iGEM community. The site-specific incorporation of ncAAs requires the directed evolution of tRNA and aminoacyl tRNA synthetase pairs, which in turn mediate the introduction of a ncAA for a certain codon. We are especially exploring the application of unnatural base pairs (UBPs) as an expansion of the genetic code. This approach promises an optimal orthogonality to the autologous translation apparatus and a high flexibility concerning the incorporation of multiple ncAAs. We will utilize several systems to achieve a high retention efficiency. As examples for the successful incorporation of non-canonical amino acids we will develop a rapid test for prions and a new chromatography method for a mild elution of proteins.
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We are exploring the application of unnatural base pairs (UBPs) as an expansion of the genetic code. To prevent loss of the unnatural base pair during reproduction we will utilize several systems including CRISPR/Cas9. The extended genetic code allows the ribosomal incorporation of several non-canonical amino acids (ncAAs) into peptides. With their broad chemical and functional diversity ncAAs provide a variety of promising applications including protein labeling, photocaging, structure analysis and specific protein interactions. Therefore, the development of a new toolkit for the translational incorporation of ncAAs in E. coli would be a great contribu-tion to the iGEM community. The site-specific incorporation of ncAAs requires the directed evolution of tRNA/aminoacyl-tRNA synthetase pairs, which in turn mediate the introduction of an ncAA for a certain codon. This approach enables an optimal orthogonality to the autologous translation apparatus and a high flexibility concern-ing the incorporation of multiple ncAAs. As examples for the successful incorporation of non-canonical amino acids, we will develop a rapid test for prions and a new chromatography method for a mild elution of proteins.
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<p>For more information visit our <b><a href="https://www.researchgate.net/publication/318084694_Expansion_of_the_genetic_code_for_the_translational_incorporation_of_non-canonical_amino_acids">project poster</a></b> on reasearch gate</p>
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<p>For more information visit our <b><a href="https://www.researchgate.net/publication/318084694_Expansion_of_the_genetic_code_for_the_translational_incorporation_of_non-canonical_amino_acids">project poster</a></b> on reasearch gate</p>
 
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Revision as of 16:23, 23 August 2017

Expanding the Genetic Code

Abstract

We are exploring the application of unnatural base pairs (UBPs) as an expansion of the genetic code. To prevent loss of the unnatural base pair during reproduction we will utilize several systems including CRISPR/Cas9. The extended genetic code allows the ribosomal incorporation of several non-canonical amino acids (ncAAs) into peptides. With their broad chemical and functional diversity ncAAs provide a variety of promising applications including protein labeling, photocaging, structure analysis and specific protein interactions. Therefore, the development of a new toolkit for the translational incorporation of ncAAs in E. coli would be a great contribu-tion to the iGEM community. The site-specific incorporation of ncAAs requires the directed evolution of tRNA/aminoacyl-tRNA synthetase pairs, which in turn mediate the introduction of an ncAA for a certain codon. This approach enables an optimal orthogonality to the autologous translation apparatus and a high flexibility concern-ing the incorporation of multiple ncAAs. As examples for the successful incorporation of non-canonical amino acids, we will develop a rapid test for prions and a new chromatography method for a mild elution of proteins.

For more information visit our project poster on reasearch gate