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Genetic incorporation of histidine derivatives using an engineered pyrrolysyl-tRNA synthetase

Academic Article
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Overview

related to degree

  • Xiao, Han, Ph.D. in Chemical Biology, Scripps Research 2010 - 2015
  • Peters, Frank, Ph.D. in Chemical Biology, Scripps Research 2006 - 2012
  • Chittuluru, Johnathan R, Ph.D. in Chemical Biology, Scripps Research 2004 - 2011

authors

  • Xiao, Han
  • Peters, Frank
  • Yang, P. Y.
  • Reed, S.
  • Chittuluru, Johnathan R
  • Schultz, Peter

publication date

  • May 2014

journal

  • ACS Chemical Biology  Journal

abstract

  • A polyspecific amber suppressor aminoacyl-tRNA synthetase/tRNA pair was evolved that genetically encodes a series of histidine analogues in both Escherichia coli and mammalian cells. In combination with tRNACUA(Pyl), a pyrrolysyl-tRNA synthetase mutant was able to site-specifically incorporate 3-methyl-histidine, 3-pyridyl-alanine, 2-furyl-alanine, and 3-(2-thienyl)-alanine into proteins in response to an amber codon. Substitution of His66 in the blue fluorescent protein (BFP) with these histidine analogues created mutant proteins with distinct spectral properties. This work further expands the structural and chemical diversity of unnatural amino acids (UAAs) that can be genetically encoded in prokaryotic and eukaryotic organisms and affords new probes of protein structure and function.

subject areas

  • Alanine
  • Amino Acyl-tRNA Synthetases
  • Escherichia coli
  • Histidine
  • Luminescent Proteins
  • Models, Molecular
  • Mutant Proteins
  • Mutation
  • Protein Engineering
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Identity

PubMed Central ID

  • PMC4033645

International Standard Serial Number (ISSN)

  • 1554-8929

Digital Object Identifier (DOI)

  • 10.1021/cb500032c

PubMed ID

  • 24506189
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Additional Document Info

start page

  • 1092

end page

  • 1096

volume

  • 9

issue

  • 5

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