| Literature DB >> 30972734 |
Hossein Amiri1,2, Harry F Noller2.
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.Entities:
Keywords: zzm321990mRNAzzm321990; helicase; mechanism; ribosome
Mesh:
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Year: 2019 PMID: 30972734 PMCID: PMC7088467 DOI: 10.1002/1873-3468.13383
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124