2010/07/07 by Harry F. Noller · 1 citation
Biochemistry, Genetics and Molecular Biology · #RNA and protein synthesis mechanisms #RNA modifications and cancer #RNA Research and Splicing
paper · pdf · doi:10.1101/cshperspect.a003681
openalex publication_date 2010/07/07 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/14
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. Outline 1 Introduction 2 Translation out of an RNA World 3 Peptidyl transferase: the ribosome is a ribozyme 4 Aminoacyl-tRNA selection: the 30S subunit a site 5 The 30S subunit p site: another function of rRNA 6 RNA molecular mechanics and translocation 7 What are ribosomal proteins for? 8 "Stop tRNAs" and the evolution of type I release factors 9 dRNA and the origins of the ribosomal decoding site 10 The driving force for evolution of translation from an RNA world 11 Conclusions