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Adding amino acids with novel reactivity to the genetic code of Saccharomyces cerevisiae

Academic Article
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Overview

related to degree

  • Anderson, John Christopher, Ph.D. in Chemistry, Scripps Research 1998 - 2003

authors

  • Deiters, A.
  • Cropp, T. A.
  • Mukherji, M.
  • Chin, J. W.
  • Anderson, John Christopher
  • Schultz, Peter

publication date

  • October 2003

journal

  • Journal of the American Chemical Society  Journal

abstract

  • Using a novel genetic selection, we have identified a series of mutants of the E. coli tyrosyl-tRNA synthetase that selectively charge an amber suppressor tRNA with p-(propargyloxy)phenylalanine and p-azidophenylalanine in yeast. These evolved tRNA-synthetase pairs can be used to site-specifically label proteins with functional groups orthogonal to normal biological chemistries. As an example, we have shown that proteins containing these amino acids can be efficiently bioconjugated with small organic molecules by a [3 + 2] cycloaddition reaction that is mild enough for the manipulation of biological samples.

subject areas

  • Acetylene
  • Amino Acids
  • Amino Acyl-tRNA Synthetases
  • Azides
  • Codon, Nonsense
  • Humans
  • Protein Engineering
  • RNA, Transfer, Amino Acid-Specific
  • Saccharomyces cerevisiae
  • Superoxide Dismutase
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Identity

International Standard Serial Number (ISSN)

  • 0002-7863

Digital Object Identifier (DOI)

  • 10.1021/ja0370037

PubMed ID

  • 14505376
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Additional Document Info

start page

  • 11782

end page

  • 11783

volume

  • 125

issue

  • 39

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