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Isomers of Aminoacyl- and Peptidyl-tRNA in the Peptidyl Transferase Reaction

  • Chapter
Structure, Function, and Genetics of Ribosomes

Part of the book series: Springer Series in Molecular Biology ((SSMOL))

Abstract

The synthesis of the peptide bonds takes place via the transfer of the activated peptidyl residue from peptidyl-tRNA to the aminoacyl residue of aa-tRNA. Although the ester bond of charged tRNAs is an energy-rich bond with the free energy of hydrolysis approximately equal to the free energy of hydrolysis of ATP (Loftfield, 1972), the reaction between peptidyl- and aminoacyl-tRNA does not occur spontaneously if the two charged tRNAs are allowed to react in buffered aqueous solutions. Even at high concentration of the charged tRNA species, a new peptide bond will not be formed in the absence of ribosomes. Therefore, the macromolecular components of the ribosomal translational apparatus must be involved either as a matrix surface or as a catalytic unit in the peptidyl transferase reaction.

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Authors
  1. M. Sprinzl
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Editors and Affiliations

  1. Clayton Foundation Biochemical Institute Department of Chemistry, The University of Texas at Austin, 78712, Austin, Texas, USA

    Boyd Hardesty  & Gisela Kramer  & 

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Sprinzl, M. (1986). Isomers of Aminoacyl- and Peptidyl-tRNA in the Peptidyl Transferase Reaction. In: Hardesty, B., Kramer, G. (eds) Structure, Function, and Genetics of Ribosomes. Springer Series in Molecular Biology. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-4884-2_29

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  • DOI: https://doi.org/10.1007/978-1-4612-4884-2_29

  • Publisher Name: Springer, New York, NY

  • Print ISBN: 978-1-4612-9346-0

  • Online ISBN: 978-1-4612-4884-2

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