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Mistranslation and its control by tRNA synthetases

Academic Article
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Overview

authors

  • Schimmel, Paul

publication date

  • October 2011

journal

  • Philosophical Transactions of the Royal Society B-Biological Sciences  Journal

abstract

  • Aminoacyl tRNA synthetases are ancient proteins that interpret the genetic material in all life forms. They are thought to have appeared during the transition from the RNA world to the theatre of proteins. During translation, they establish the rules of the genetic code, whereby each amino acid is attached to a tRNA that is cognate to the amino acid. Mistranslation occurs when an amino acid is attached to the wrong tRNA and subsequently is misplaced in a nascent protein. Mistranslation can be toxic to bacteria and mammalian cells, and can lead to heritable mutations. The great challenge for nature appears to be serine-for-alanine mistranslation, where even small amounts of this mistranslation cause severe neuropathologies in the mouse. To minimize serine-for-alanine mistranslation, powerful selective pressures developed to prevent mistranslation through a special editing activity imbedded within alanyl-tRNA synthetases (AlaRSs). However, serine-for-alanine mistranslation is so challenging that a separate, genome-encoded fragment of the editing domain of AlaRS is distributed throughout the Tree of Life to redundantly prevent serine-to-alanine mistranslation. Detailed X-ray structural and functional analysis shed light on why serine-for-alanine mistranslation is a universal problem, and on the selective pressures that engendered the appearance of AlaXps at the base of the Tree of Life.

subject areas

  • Amino Acids
  • Amino Acyl-tRNA Synthetases
  • Animals
  • Catalytic Domain
  • Electrophoretic Mobility Shift Assay
  • Genetic Code
  • Humans
  • Mammals
  • Mice
  • Nucleotides
  • Protein Biosynthesis
  • RNA Editing
  • RNA, Transfer, Amino Acyl
  • Transfer RNA Aminoacylation
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Research

keywords

  • editing
  • genetic code
  • serine-for-alanine mistranslation
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Identity

PubMed Central ID

  • PMC3158927

International Standard Serial Number (ISSN)

  • 0962-8436

Digital Object Identifier (DOI)

  • 10.1098/rstb.2011.0158

PubMed ID

  • 21930589
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Additional Document Info

start page

  • 2965

end page

  • 2971

volume

  • 366

issue

  • 1580

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