Tracking fluctuation hotspots on the yeast ribosome through the elongation cycle

Nucleic Acids Res. 2017 May 5;45(8):4958-4971. doi: 10.1093/nar/gkx112.

Abstract

Chemical modification was used to quantitatively determine the flexibility of nearly the entire rRNA component of the yeast ribosome through 8 discrete stages of translational elongation, revealing novel observations at the gross and fine-scales. These include (i) the bulk transfer of energy through the intersubunit bridges from the large to the small subunit after peptidyltransfer, (ii) differences in the interaction of the sarcin ricin loop with the two elongation factors and (iii) networked information exchange pathways that may functionally facilitate intra- and intersubunit coordination, including the 5.8S rRNA. These analyses reveal hot spots of fluctuations that set the stage for large-scale conformational changes essential for translocation and enable the first molecular dynamics simulation of an 80S complex. Comprehensive datasets of rRNA base flexibilities provide a unique resource to the structural biology community that can be computationally mined to complement ongoing research toward the goal of understanding the dynamic ribosome.

MeSH terms

  • Binding Sites
  • Molecular Dynamics Simulation
  • Nucleic Acid Conformation
  • Peptide Chain Elongation, Translational*
  • Peptide Elongation Factors / chemistry
  • Peptide Elongation Factors / genetics
  • Protein Biosynthesis / genetics
  • RNA, Ribosomal / chemistry
  • RNA, Ribosomal / genetics
  • RNA, Ribosomal, 5.8S / chemistry*
  • RNA, Ribosomal, 5.8S / genetics
  • Ribosomes / chemistry
  • Ribosomes / genetics*
  • Saccharomyces cerevisiae / chemistry
  • Saccharomyces cerevisiae / genetics

Substances

  • Peptide Elongation Factors
  • RNA, Ribosomal
  • RNA, Ribosomal, 5.8S