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Cold Spring Harb Perspect Biol. 2012 Apr 1;4(4):a003681. doi: 10.1101/cshperspect.a003681.

Evolution of protein synthesis from an RNA world.

Author information

1
Center for Molecular Biology of RNA and Department of Molecular, Cell, and Developmental Biology, Sinsheimer Laboratories, University of California at Santa Cruz, Santa Cruz, California 95064, USA. harry@nuvolari.ucsc.edu

Abstract

Because of the molecular complexity of the ribosome and protein synthesis, it is a challenge to imagine how translation could have evolved from a primitive RNA World. Two specific suggestions are made here to help to address this, involving separate evolution of the peptidyl transferase and decoding functions. First, it is proposed that translation originally arose not to synthesize functional proteins, but to provide simple (perhaps random) peptides that bound to RNA, increasing its available structure space, and therefore its functional capabilities. Second, it is proposed that the decoding site of the ribosome evolved from a mechanism for duplication of RNA. This process involved homodimeric "duplicator RNAs," resembling the anticodon arms of tRNAs, which directed ligation of trinucleotides in response to an RNA template.

PMID:
20610545
PMCID:
PMC3312679
DOI:
10.1101/cshperspect.a003681
[Indexed for MEDLINE]
Free PMC Article

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