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Cellular and Molecular Life Sciences: CMLS logoLink to Cellular and Molecular Life Sciences: CMLS
. 2004 May;61(11):1317–1330. doi: 10.1007/s00018-004-3449-9

Peptide synthesis through evolution

K Tamura 1,, R W Alexander 2,
PMCID: PMC11138682  PMID: 15170510

Abstract

Ribosome-catalyzed peptide bond formation is a crucial function of all organisms. The ribosome is a ribonucleoprotein particle, with both RNA and protein components necessary for the various steps leading to protein biosynthesis. Evolutionary theory predicts an early environment devoid of complex biomolecules, and prebiotic peptide synthesis would have started in a simple way. A fundamental question regarding peptide synthesis is how the current ribosome-catalyzed reaction evolved from a primitive system. Here we look at both prebiotic and modern mechanisms of peptide bond formation and discuss recent experiments that aim to connect these activities. In particular, RNA can facilitate peptide bond formation by providing a template for activated amino acids to react and can catalyze a variety of functions that would have been necessary in a pre-protein world. Therefore, RNA may have facilitated the emergence of the current protein world from an RNA or even prebiotic world.

Keywords: Peptide bond formation, ribosome, tRNA, minihelix, RNA world, oligonucleotides, template, evolution, prebiotic

Footnotes

Received 4 December 2003; received after revision 13 January 2004; accepted 15 January 2004

Contributor Information

K. Tamura, Email: tamura@scripps.edu

R. W. Alexander, Email: alexanr@wfu.edu


Articles from Cellular and Molecular Life Sciences: CMLS are provided here courtesy of Springer

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