rpsA and ribosomal protein S1: investigating a non-canonical translation initiation element

Translation initiation rates are fine-tuned by altering interactions between the ribosome and the translation initiation region of an mRNA. In bacteria varying levels of RNA structure attenuate these interactions by masking the ribosome-binding site from the small ribosomal subunit. Recent studies have described diverse strategies for recruiting mRNA to the ribosome, and highlighted the contributions of ribosomal protein S1. Here, I provide evidence that the non-canonical initiation mechanism that governs translation of the rpsA mRNA, encoding ribosomal protein S1, contains a three-dimensional architecture that is required for efficient translation. Furthermore, S1 plays an essential role during the initiation phase of translation by recruiting mRNA to the ribosome—unfolding structured mRNAs, and allowing for correct start codon positioning on the ribosome. Combining crosslinking immunoprecipitation and high-throughput sequencing approaches revealed the extent of S1’s involvement in mRNA recruitment, while also highlighting a broader role as a regulator of many RNA classes.

Authors

• Vigar, Justin R. J.
• University of Lethbridge. Faculty of Arts and Science

• RNA
• Biophysics
• Synthetic Biology
• Ribosome
• Translation Initiation
• Engineering
• RNA-seq
• Dissertations, Academic

Identifier

hdl:10133/5670

OAI identifier oai:identifier

oai:opus.uleth.ca:10133/5670