Evolution of protein synthesis from an RNA world

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...

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Bibliographic Details
Published in:Cold Spring Harbor perspectives in biology 2012-04, Vol.4 (4), p.a003681-a003681
Main Author: Noller, Harry F
Format: Article
Language:English
Subjects:
Anticodons
Biological Evolution
Concepts
Evolution
Nucleic Acid Conformation
Peptidyltransferase
Protein Biosynthesis
Ribosomes
RNA
RNA - chemistry
RNA - genetics
Transcription
Translation
tRNA
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Summary: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.
ISSN:1943-0264
1943-0264
DOI:10.1101/cshperspect.a003681