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Aminoacyl tRNA synthetases and their connections to disease

Academic Article
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Overview

authors

  • Park, S. G.
  • Schimmel, Paul
  • Kim, S.

publication date

  • August 2008

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • Aminoacylation of transfer RNAs establishes the rules of the genetic code. The reactions are catalyzed by an ancient group of 20 enzymes (one for each amino acid) known as aminoacyl tRNA synthetases (AARSs). Surprisingly, the etiology of specific diseases-including cancer, neuronal pathologies, autoimmune disorders, and disrupted metabolic conditions-is connected to specific aminoacyl tRNA synthetases. These connections include heritable mutations in the genes for tRNA synthetases that are causally linked to disease, with both dominant and recessive disease-causing mutations being annotated. Because some disease-causing mutations do not affect aminoacylation activity or apparent enzyme stability, the mutations are believed to affect functions that are distinct from aminoacylation. Examples include enzymes that are secreted as procytokines that, after activation, operate in pathways connected to the immune system or angiogenesis. In addition, within cells, synthetases form multiprotein complexes with each other or with other regulatory factors and in that way control diverse signaling pathways. Although much has been uncovered in recent years, many novel functions, disease connections, and interpathway connections of tRNA synthetases have yet to be worked out.

subject areas

  • Amino Acyl-tRNA Synthetases
  • Animals
  • Autoimmune Diseases
  • Cytokines
  • Enzyme Stability
  • Humans
  • Metabolic Diseases
  • Multienzyme Complexes
  • Mutation
  • Neoplasms
  • Neovascularization, Pathologic
  • Nervous System Diseases
  • Transfer RNA Aminoacylation
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Research

keywords

  • AIMP
  • multifunctional protein
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Identity

PubMed Central ID

  • PMC2516211

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.0802862105

PubMed ID

  • 18682559
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Additional Document Info

start page

  • 11043

end page

  • 11049

volume

  • 105

issue

  • 32

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