AI Article Synopsis
- The study investigates how introns are removed from pre-tRNAs across all living organisms, highlighting the importance of this process in tRNA maturation and functionality.* -
- The researchers present a detailed cryo-EM structure of the active human tRNA splicing endonuclease complex, showing how specific components recognize pre-tRNA and prepare it for splicing.* -
- The findings provide insights into the molecular mechanism of pre-tRNA recognition and cleavage, while also showing evolutionary connections between proteins in archaea and eukaryotes.*
Article Abstract
Removal of introns from transfer RNA precursors (pre-tRNAs) occurs in all living organisms. This is a vital phase in the maturation and functionality of tRNA. Here we present a 3.2 Å-resolution cryo-EM structure of an active human tRNA splicing endonuclease complex bound to an intron-containing pre-tRNA. TSEN54, along with the unique regions of TSEN34 and TSEN2, cooperatively recognizes the mature body of pre-tRNA and guides the anticodon-intron stem to the correct position for splicing. We capture the moment when the endonucleases are poised for cleavage, illuminating the molecular mechanism for both 3' and 5' cleavage reactions. Two insertion loops from TSEN54 and TSEN2 cover the 3' and 5' splice sites, respectively, trapping the scissile phosphate in the center of the catalytic triad of residues. Our findings reveal the molecular mechanism for eukaryotic pre-tRNA recognition and cleavage, as well as the evolutionary relationship between archaeal and eukaryotic TSENs.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10539383 | PMC |
| http://dx.doi.org/10.1038/s41467-023-41845-y | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!