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Cell-type-specific translational regulation by human DUS enzymes [tRNA DESeq]

ABSTRACT: Cell-type-specific translational regulation by human DUS enzymes [tRNA DESeq]

PROVIDER: PRJNA1034643 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR26632724_1.fastq.gz	Fastqsanger.gz
	SRR26632724_2.fastq.gz	Fastqsanger.gz
	SRR26632725_1.fastq.gz	Fastqsanger.gz
	SRR26632725_2.fastq.gz	Fastqsanger.gz
	SRR26632726_1.fastq.gz	Fastqsanger.gz

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Cell-type-specific translational regulation by human DUS enzymes [tRNA NaBH4]

Project description:Dihydrouridine is an abundant and evolutionary conserved modified nucleoside present on tRNA, but characterization and functional studies of individual modification sites and associated DUS writer enzymes in mammals is lacking. Here we use a chemical probing strategy, RNABPP-PS, to identify 5-chlorouridine as a general activity-based probe for human DUS enzymes. We map D modifications using mechanism-based RNA-protein crosslinking and also through chemical reactivity and mutational profiling to reveal the landscape of D modification sites on human tRNAs. Further, we knockout individual DUS genes in two model human cell lines to investigate their regulation of tRNA expression levels and codon-specific translation elongation. We show that whereas D modifications are present across most tRNA species, loss of D only perturbs the translational function of a subset of tRNAs in a cell-type-specific manner. Our work provides powerful chemical strategies for investigating D and DUS enzymes in diverse biological systems and provides insight into the role of a ubiquitous tRNA modification in translational regulation.

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Cell-type-specific translational regulation by human DUS enzymes [tRNA NaBH4]

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Cell-type-specific translational regulation by human DUS enzymes

Project description:Cell-type-specific translational regulation by human DUS enzymes

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Regulation of Ex-Translational Activities Is Primary Function of Multi-tRNA Synthetase Complex

Project description:During mRNA translation, tRNAs are charged by aminoacyl-tRNA synthetases (aaRS) and subsequently used by ribosomes. A multi-enzyme aminoacyl-tRNA synthetase complex (MSC) has long been proposed to increase protein synthesis efficiency by passing charged tRNAs directly to ribosomes. An alternative is that the MSC repurposes specific synthetases for ex-translational functions that are activated by cues that direct specific enzymes to novel targets. To explore this question, we generated mammalian cell clones in which ArgRS and GlnRS were absent from the MSC to give a stable complex lacking the two enzymes (MSCΔRQ). Protein synthesis, under a variety of stress conditions, was unchanged in MSCΔRQ cells. Most strikingly, levels of charged tRNAGln and tRNAArg remained unchanged and no ribosome pausing was observed at codons for Arg and Gln. Thus, increasing or regulating protein synthesis efficiency is not dependent on ArgRS and GlnRS in the MSC. Alternatively, and consistent with previously reported ex-translational roles, we found manipulations that do not affect protein synthesis but instead MSC cellular localization.

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A multiplex platform for small RNA sequencing elucidates multifaceted tRNA stress response and translational regulation

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