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Mutational switching of a yeast tRNA synthetase into a mammalian-like synthetase cytokine

Academic Article
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Overview

authors

  • Liu, J. M.
  • Yang, Xiang-Lei
  • Ewalt, K. L.
  • Schimmel, Paul

publication date

  • December 2002

journal

  • Biochemistry  Journal

abstract

  • Aminoacyl-tRNA synthetases catalyze the attachment of amino acids to their cognate tRNAs. A link was recently established between protein biosynthesis and cytokine signal transduction. Human tyrosyl-tRNA synthetase can be split into two fragments, each of which has a distinct cytokine function. This activity is specific to the human enzyme. It is absent in the enzymes from lower organisms such as bacteria and yeast. Here, yeast tyrosyl-tRNA synthetase (TyrRS), which lacks cytokine activity, was used as a model to explore how a human tyrosyl-tRNA synthetase during evolution acquired novel functions beyond aminoacylation. We found that a rationally designed mutant yeast TyrRS(ELR) gained cytokine function. The mutant yeast enzyme gained this function without sacrifice of aminoacylation activity. Therefore, relatively simple alteration of a basic structural motif imparts cytokine activity to a tRNA synthetase while preserving its canonical function. Further work established that mutational switching of a yeast protein to a mammalian-like cytokine was specific to this synthetase and not to just any yeast ortholog of a mammalian cytokine.

subject areas

  • Acylation
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Chemotaxis, Leukocyte
  • Cytokines
  • Humans
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Neoplasm Proteins
  • Neutrophils
  • RNA-Binding Proteins
  • Recombinant Proteins
  • Saccharomyces cerevisiae Proteins
  • Tyrosine-tRNA Ligase
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Identity

International Standard Serial Number (ISSN)

  • 0006-2960

Digital Object Identifier (DOI)

  • 10.1021/bi0205395

PubMed ID

  • 12450387
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Additional Document Info

start page

  • 14232

end page

  • 14237

volume

  • 41

issue

  • 48

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