Recurring RNA structural motifs underlie the mechanics of L1 stalk movement.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 28176782.
- Also identified by DOI 10.1038/ncomms14285 and PMC identifier 5309774.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
The L1 stalk of the large ribosomal subunit undergoes large-scale movements coupled to the translocation of deacylated tRNA during protein synthesis. We use quantitative comparative structural analysis to localize the origins of L1 stalk movement and to understand its dynamic interactions with tRNA and other structural elements of the ribosome. Besides its stacking interactions with the tRNA elbow, stalk movement is directly linked to intersubunit rotation, rotation of the 30S head domain and contact of the acceptor arm of deacylated tRNA with helix 68 of 23S rRNA. Movement originates from pivoting at stacked non-canonical base pairs in a Family A three-way junction and bending in an internal G-U-rich zone. Use of these same motifs as hinge points to enable such dynamic events as rotation of the 30S subunit head domain and in flexing of the anticodon arm of tRNA suggests that they represent general strategies for movement of functional RNAs.
Medical subject headings
- Nucleotide Motifs
- Protein Biosynthesis
- RNA, Ribosomal, 23S
- RNA, Transfer
- Ribosome Subunits, Large