Document Type
Article
Publication Date
8-11-2025
Abstract
RNA post-transcriptional modifications act by stabilizing the functional conformations of RNA. While their role in messenger RNA (mRNA) decoding is well established, it is less clear how transfer RNA (tRNA) modifications outside the anticodon contribute to tRNA stability and accurate protein synthesis. Absence of such modifications causes translation errors, including mRNA frameshifting. By integrating single-molecule fluorescence resonance energy transfer and cryogenic electron microscopy, we demonstrate that the N1-methylguanosine (m1G) modification at position 37 of Escherichia coli tRNAProL is necessary and sufficient for modulating the conformational energy of this tRNA on the ribosome so as to suppress +1 frameshifting otherwise induced by this tRNA. Six structures of E. coli ribosomal complexes carrying tRNAProL lacking m1G37 show this tRNA forms four and even five codon-anticodon base pairs as it moves into the +1 frame, allowing direct visualization of the long-standing hypothesis that a four base pair codon-anticodon can form during +1 frameshifting.
Recommended Citation
Kimbrough, Evelyn M.; Nguyen, Ha An; Li, Haixing; Mattingly, Jacob M.; Bailey, Nevette A.; Ning, Wei; Gamper, Howard; Hou, Ya-Ming; Gonzalez, Ruben L.; and Dunham, Christine M., "An Rna Modification Prevents Extended Codon-Anticodon Interactions From Facilitating +1 Frameshifting" (2025). Department of Biochemistry and Molecular Biology Faculty Papers. Paper 286.
https://jdc.jefferson.edu/bmpfp/286
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.
PubMed ID
40789848
Language
English
Comments
This article is the author's final published version in Nature Communications, Volume 16, Issue 1, August 2025, Article number 7392.
The published version is available at https://doi.org/10.1038/s41467-025-62342-4. Copyright © The Author(s).