Insights into genome recoding from the mechanism of a classic +1-frameshifting tRNA

Howard Gamper, Haixing Li, Isao Masuda, D. Miklos Robkis, Thomas Christian, Adam B. Conn, Gregor Blaha, E. James Petersson, Ruben L. Gonzalez () and Ya-Ming Hou ()
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Howard Gamper: Thomas Jefferson University
Haixing Li: Columbia University
Isao Masuda: Thomas Jefferson University
D. Miklos Robkis: University of Pennsylvania
Thomas Christian: Thomas Jefferson University
Adam B. Conn: University of California
Gregor Blaha: University of California
E. James Petersson: University of Pennsylvania
Ruben L. Gonzalez: Columbia University
Ya-Ming Hou: Thomas Jefferson University

Nature Communications, 2021, vol. 12, issue 1, 1-18

Abstract: Abstract While genome recoding using quadruplet codons to incorporate non-proteinogenic amino acids is attractive for biotechnology and bioengineering purposes, the mechanism through which such codons are translated is poorly understood. Here we investigate translation of quadruplet codons by a +1-frameshifting tRNA, SufB2, that contains an extra nucleotide in its anticodon loop. Natural post-transcriptional modification of SufB2 in cells prevents it from frameshifting using a quadruplet-pairing mechanism such that it preferentially employs a triplet-slippage mechanism. We show that SufB2 uses triplet anticodon-codon pairing in the 0-frame to initially decode the quadruplet codon, but subsequently shifts to the +1-frame during tRNA-mRNA translocation. SufB2 frameshifting involves perturbation of an essential ribosome conformational change that facilitates tRNA-mRNA movements at a late stage of the translocation reaction. Our results provide a molecular mechanism for SufB2-induced +1 frameshifting and suggest that engineering of a specific ribosome conformational change can improve the efficiency of genome recoding.

Date: 2021
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DOI: 10.1038/s41467-020-20373-z

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