An RNA modification prevents extended codon-anticodon interactions from facilitating +1 frameshifting

Evelyn M. Kimbrough, Ha An Nguyen, Haixing Li, Jacob M. Mattingly, Nevette A. Bailey, Wei Ning, Howard Gamper, Ya-Ming Hou, Ruben L. Gonzalez () and Christine M. Dunham ()
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Evelyn M. Kimbrough: Emory University
Ha An Nguyen: Emory University
Haixing Li: Columbia University
Jacob M. Mattingly: Emory University
Nevette A. Bailey: Columbia University
Wei Ning: Columbia University
Howard Gamper: Thomas Jefferson University
Ya-Ming Hou: Thomas Jefferson University
Ruben L. Gonzalez: Columbia University
Christine M. Dunham: Emory University

Nature Communications, 2025, vol. 16, issue 1, 1-13

Abstract: 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.

Date: 2025
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DOI: 10.1038/s41467-025-62342-4

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