Altered tRNA processing is linked to a distinct and unusual La protein in Tetrahymena thermophila

Kyra Kerkhofs, Jyoti Garg, Étienne Fafard-Couture, Sherif Abou Elela, Michelle S. Scott, Ronald E. Pearlman and Mark A. Bayfield ()
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Kyra Kerkhofs: York University
Jyoti Garg: York University
Étienne Fafard-Couture: Université de Sherbrooke
Sherif Abou Elela: Université de Sherbrooke
Michelle S. Scott: Université de Sherbrooke
Ronald E. Pearlman: York University
Mark A. Bayfield: York University

Nature Communications, 2022, vol. 13, issue 1, 1-17

Abstract: Abstract Nascent pre-tRNAs are transcribed by RNA polymerase III and immediately bound by La proteins on the UUU-3’OH sequence, using a tandem arrangement of the La motif and an adjacent RNA recognition motif-1 (RRM1), resulting in protection from 3’-exonucleases and promotion of pre-tRNA folding. The Tetrahymena thermophila protein Mlp1 has been previously classified as a genuine La protein, despite the predicted absence of the RRM1. We find that Mlp1 functions as a La protein through binding of pre-tRNAs, and affects pre-tRNA processing in Tetrahymena thermophila and when expressed in fission yeast. However, unlike in other examined eukaryotes, depletion of Mlp1 results in 3’-trailer stabilization. The 3’-trailers in Tetrahymena thermophila are uniquely short relative to other examined eukaryotes, and 5’-leaders have evolved to disfavour pre-tRNA leader/trailer pairing. Our data indicate that this variant Mlp1 architecture is linked to an altered, novel mechanism of tRNA processing in Tetrahymena thermophila.

Date: 2022
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DOI: 10.1038/s41467-022-34796-3

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