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TRMT1L-catalyzed m22G27 on tyrosine tRNA is required for efficient mRNA translation and cell survival under oxidative stress. [eCLIP-seq]

ABSTRACT: TRMT1L-catalyzed m22G27 on tyrosine tRNA is required for efficient mRNA translation and cell survival under oxidative stress. [eCLIP-seq]

PROVIDER: PRJNA1107680 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR28891684_1.fastq.gz	Fastqsanger.gz
	SRR28891684_2.fastq.gz	Fastqsanger.gz
	SRR28891685_1.fastq.gz	Fastqsanger.gz
	SRR28891685_2.fastq.gz	Fastqsanger.gz
	SRR28891686_1.fastq.gz	Fastqsanger.gz

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TRMT1L-catalyzed m22G27 on tyrosine tRNA is required for efficient mRNA translation and cell survival under oxidative stress. [eCLIP-seq]

Project description:Mapping of the epitranscriptome has revealed the chemical diversity of RNA modifications and their functional importance in regulating gene expression. Transfer RNAs (tRNAs) are one of the most modified cellular RNAs, containing on average 10-13 modifications per molecule. These modifications have been shown to be critical for several aspects of tRNA functions, such as decoding, folding, and stability. Here we report that the human RNA methyltransferase TRMT1L associates with components of the Rix1 ribosome biogenesis complex and co-sediments with pre-60S ribosomes. Using eCLIP-Seq, we show that TRMT1L binds to a subset of tRNAs and to the 28S rRNA. Additionally, we demonstrate that TRMT1L is responsible for catalyzing N2, N2-dimethylguanosine (m22G) solely at position 27 of tRNA-Tyr-GUA by Nano-tRNAseq and RNA LC-MS. Surprisingly, TRMT1L depletion also impaired the deposition of acp3U and dihydrouridine on tRNA-Tyr-GUA, Cys-GCA, and Ala-CGC. TRMT1L knockout cells have a marked decrease in tRNA-Tyr-GUA levels, coinciding with a reduction in global translation rates and hypersensitivity of oxidative stress. Our results establish TRMT1L as the elusive methyltransferase catalyzing the m22G27 modification on tRNA Tyr, resolving a long-standing gap of knowledge and highlighting its potential role in a tRNA modification circuit crucial for translation regulation and stress response.

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TRMT1L-catalyzed m22G27 on tyrosine tRNA is required for efficient mRNA translation and cell survival under oxidative stress. [Nano-tRNAseq]

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TRMT1L-catalyzed m22G27 on tyrosine tRNA is required for efficient mRNA translation and cell survival under oxidative stress. [Nano-tRNAseq]

Project description:TRMT1L-catalyzed m22G27 on tyrosine tRNA is required for efficient mRNA translation and cell survival under oxidative stress. [Nano-tRNAseq]

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Elucidating the human tRNA transcriptome dependent upon the TRMT1 and TRMT1L paralogs for modification, stability, and function

Project description:The tRNA methyltransferase 1 (TRMT1) enzyme catalyzes the formation of dimethylguanosine (m2,2G) in tRNAs. Loss-of-function mutations in TRMT1 lead to intellectual disability disorders in humans. In addition to TRMT1, vertebrates encode a tRNA methyltransferase 1-like (TRMT1L) paralog. Here, we use a comprehensive tRNA sequencing approach to decipher the landscape of tRNAs that are modified by human TRMT1 and TRMT1L. We find that TRMT1 modifies a single position in more than half of all cytoplasmic tRNAs and a subset of mitochondrial tRNAs. Notably, TRMT1 and TRMT1L catalyze m2,2G formation at distinct positions in tyrosine tRNAs that are each required for the efficient installation of additional modifications. Moreover, we identify a role for m2,2G modification in the stability of tyrosine and serine tRNAs that is abrogated in human patient cells homozygous for pathogenic TRMT1 variants. Human cells deficient in TRMT1 and/or TRMT1L exhibit reduced translation of specific codons, indicating that m2,2G modifications are necessary for maintaining functional levels of certain tRNAs. These findings uncover key roles for the m2,2G modification, and pinpoint tRNAs that are dysregulated in neurodevelopmental disorders caused by tRNA modification deficiency.

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Project description: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 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 m2 2G solely at position 27 of tRNA-Tyr-GUA. Surprisingly, TRMT1L depletion also impaired the deposition of acp3U and dihydrouridine on tRNA-Tyr-GUA, Cys-GCA, and Ala-CGC. TRMT1L knockout cells have a marked decrease in tRNA-Tyr-GUA levels, coinciding with a reduction in global translation rates and hypersensitivity to oxidative stress. Our results establish TRMT1L as the elusive methyltransferase catalyzing the m2 2G27 modification on tRNA Tyr, resolving a long-standing gap of knowledge and highlighting its potential role in a tRNA modification circuit crucial for translation regulation and stress response.

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