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Emergence and Evolution

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Book cover Aminoacyl-tRNA Synthetases in Biology and Medicine

Part of the book series: Topics in Current Chemistry ((TOPCURRCHEM,volume 344))

Abstract

The aminoacyl-tRNA synthetases (aaRSs) are essential components of the protein synthesis machinery responsible for defining the genetic code by pairing the correct amino acids to their cognate tRNAs. The aaRSs are an ancient enzyme family believed to have origins that may predate the last common ancestor and as such they provide insights into the evolution and development of the extant genetic code. Although the aaRSs have long been viewed as a highly conserved group of enzymes, findings within the last couple of decades have started to demonstrate how diverse and versatile these enzymes really are. Beyond their central role in translation, aaRSs and their numerous homologs have evolved a wide array of alternative functions both inside and outside translation. Current understanding of the emergence of the aaRSs, and their subsequent evolution into a functionally diverse enzyme family, are discussed in this chapter.

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Notes

  1. 1.

    Specific aminoacyl-tRNA synthetases are denoted by their three-letter amino acid designation, e.g., LysRS for lysyl-tRNA synthetase. Lysine tRNA or tRNALys denote uncharged tRNA specific for lysine; lysyl-tRNA or Lys-tRNA denote tRNA aminoacylated with lysine.

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    Tammy J. Bullwinkle & Michael Ibba

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    Sunghoon Kim

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Bullwinkle, T.J., Ibba, M. (2013). Emergence and Evolution. In: Kim, S. (eds) Aminoacyl-tRNA Synthetases in Biology and Medicine. Topics in Current Chemistry, vol 344. Springer, Dordrecht. https://doi.org/10.1007/128_2013_423

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