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Bacteria use unique mRNA features for translation initiation, lacking Shine-Dalgarno sequences. This study reveals how ribosome protein bS21 regulates translation of its own gene, rpsU, impacting bacterial gene expression.

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Area of Science:

  • Molecular Biology
  • Bacterial Genetics
  • Structural Biology

Background:

  • Bacteria of the class Bacteroidia initiate translation using messenger RNA (mRNA) features distinct from the canonical Shine-Dalgarno (SD) sequence.
  • Bacteroidia ribosomes possess an anti-SD (ASD) sequence in their 16S ribosomal RNA (rRNA), which is typically sequestered by ribosomal proteins bS21, bS18, and bS6, rendering them insensitive to SD sequences.

Purpose of the Study:

  • To investigate the structural mechanisms governing translation initiation on the rpsU mRNA in Bacteroidia.
  • To elucidate how the ribosomal protein bS21 autoregulates the translation of its own gene, rpsU.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was employed to determine the structure of the translation initiation complex on rpsU mRNA.
  • Site-directed mutagenesis was used to probe the roles of bS21, bS18, and bS6 in regulating translation initiation.

Main Results:

  • Initiation on rpsU mRNA involves the formation of a Shine-Dalgarno (SD)-anti-SD (ASD) helix, which sterically hinders the binding of ribosomal protein bS21.
  • Mutations disrupting the bS21, bS18, or bS6 binding pocket release the 16S rRNA 3' tail, facilitating SD-ASD pairing and enhancing translation initiation.
  • The dissociation of bS21 from ribosomes is inferred to control the rate of rpsU mRNA initiation.

Conclusions:

  • Ribosome composition, specifically the presence or absence of bS21, dictates translation initiation on specific mRNAs like rpsU.
  • This autoregulatory mechanism provides a unique strategy for controlling gene expression in Bacteroidia.
  • The findings highlight how structural interactions within the ribosome can modulate translation of essential genes.