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tRNA modifications are critical for several aspects of their functions, including decoding, folding, and stability. Using a multifaceted approach encompassing eCLIP-seq and nanopore tRNA-seq, we show that the human tRNA methyltransferase TRMT1L interacts with the component of the Rix1 ribosome biogenesis complex and binds to the 28S rRNA as well as to a subset of tRNAs. Mechanistically, we demonstrate that TRMT1L is responsible for catalyzing N2,N2-dimethylguanosine (mG) solely at position 27 of tRNA-Tyr-GUA.

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The tRNA methyltransferase 1 (TRMT1) enzyme catalyzes the N2,N2-dimethylguanosine (m2,2G) modification in tRNAs. Intriguingly, vertebrates encode an additional tRNA methyltransferase 1-like (TRMT1L) paralog. Here, we use a comprehensive tRNA sequencing approach to decipher targets of human TRMT1 and TRMT1L.

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The SARS-CoV-2 main protease (M or Nsp5) is critical for production of viral proteins during infection and, like many viral proteases, also targets host proteins to subvert their cellular functions. Here, we show that the human tRNA methyltransferase TRMT1 is recognized and cleaved by SARS-CoV-2 M. TRMT1 installs the ,-dimethylguanosine (m2,2G) modification on mammalian tRNAs, which promotes cellular protein synthesis and redox homeostasis.

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2-methylguanosine is an eukaryote-specific modified nucleoside in transfer RNAs, and mG10 is catalyzed by Trm11-Trm112 protein complex in eukaryotic tRNAs. Here, we show that loss-of-function mutation of the Arabidopsis Trm11 homolog AtTRM11 resulted in mG deficiency associated with disturbed ribosome assembly and overall transcriptome changes, including genes involved in flowering regulation and plant-pathogen interaction. The attrm11 mutant showed phenotypes of enlarged rosette leaves and early flowering, as well as enhanced resistance to Pseudomonas bacterial infection.

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Fine particulate matter (PM2.5) exposure has been associated with increased incidence and mortality of lung cancer. However, the molecular mechanisms underlying PM2.

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