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A genetically encoded metabolically stable analogue of phosphotyrosine in Escherichia coli

Academic Article
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Overview

related to degree

  • Xie, Jianming, Ph.D. in Chemistry, Scripps Research 2001 - 2006

authors

  • Xie, Jianming
  • Supekova, L.
  • Schultz, Peter

publication date

  • July 2007

journal

  • ACS Chemical Biology  Journal

abstract

  • p-Carboxymethyl- l-phenylalanine (pCMF), a phosphotyrosine (pTyr) mimetic that is resistant to protein tyrosine phosphatase hydrolysis, was cotranslationally incorporated into proteins in Escherichia coli using an orthogonal amber suppressor tRNA/aminoacyl-tRNA synthetase (aaRS) pair. The pCMF-specific aaRS was identified from a large library of Methanococcus jannaschii tyrosyl-tRNA synthetase active-site mutants by a combination of positive and negative genetic selections. When pCMF was substituted for Tyr701 in human signal transducer and activator of transcription-1 (STAT1), a constitutively active mutant was obtained that dimerizes and binds a DNA oligonucleotide duplex that contains the M67 site recognized by Tyr701-phosphorylated STAT1. Genetic incorporation of pCMF into proteins should provide a new tool for the preparation of stable analogues of a wide array of phosphoproteins involved in signal transduction pathways, as well as the development of peptide-based, cellularly expressed inhibitors of pTyr binding proteins.

subject areas

  • Dimerization
  • Escherichia coli
  • Phosphorylation
  • Phosphotyrosine
  • STAT1 Transcription Factor
  • Signal Transduction
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Identity

International Standard Serial Number (ISSN)

  • 1554-8929

Digital Object Identifier (DOI)

  • 10.1021/cb700083w

PubMed ID

  • 17622177
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Additional Document Info

start page

  • 474

end page

  • 478

volume

  • 2

issue

  • 7

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