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Updated: Jan 26, 2026

Chromatographic Purification of Highly Active Yeast Ribosomes
Published on: October 24, 2011
A tandem active site model for the ribosomal helicase
Hossein Amiri1,2, Harry F Noller2
1Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA, USA.
Abstract:
During protein synthesis, the messenger RNA (mRNA) helicase activity of the ribosome ensures that codons are made single stranded before decoding. Here, based on recent structural and functional findings, a quantitative model is presented for a tandem arrangement of two helicase active sites on the ribosome. A distal site encounters mRNA structures first, one elongation cycle earlier than a proximal site. Although unwinding of encountered mRNA structures past the proximal site is required for translocation, two routes exist for translocation past the distal site: sliding, which requires unwinding, and stick-slip, which does not. The model accounts in detail for a number of findings related to the ribosomal helicase and provides a testable framework to further study mRNA unwinding.
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