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Translation in amino acid-poor environments is limited by tRNAGln charging

ABSTRACT: Translation in amino acid-poor environments is limited by tRNAGln charging

PROVIDER: PRJNA660742 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR12564265_1.fastq.gz	Fastqsanger.gz
	SRR12564265_2.fastq.gz	Fastqsanger.gz
	SRR12564266_1.fastq.gz	Fastqsanger.gz
	SRR12564266_2.fastq.gz	Fastqsanger.gz
	SRR12564267_1.fastq.gz	Fastqsanger.gz

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Translation in amino acid-poor environments is limited by tRNAGln charging

Project description:An inadequate supply of amino acids leads to accumulation of uncharged tRNAs, which can bind and activate GCN2 kinase to reduce translation. Here, we show that glutamine-specific tRNAs selectively become uncharged when extracellular amino acid availability is compromised. In contrast, all other tRNAs retain charging of their cognate amino acids in a manner that is dependent upon intact lysosomal function. In addition to GCN2 activation and reduced total translation, the reduced charging of tRNAGln in amino acid-deprived cells also leads to specific depletion of proteins containing polyglutamine tracts including core binding factor α1, mediator subunit 12, transcriptional coactivator CBP and TATA-box binding protein. Treating amino acid-deprived cells with exogenous glutamine or glutaminase inhibitors restores tRNAGln charging and the levels of polyglutamine-containing proteins. Together, these results demonstrate that the activation of GCN2 and the translation of polyglutamine-encoding transcripts serve as the key sensors of glutamine availability in mammalian cells.

2020-12-14 | GSE157276 | GEO

Translation in amino-acid-poor environments is limited by tRNAGln charging.

Project description:An inadequate supply of amino acids leads to accumulation of uncharged tRNAs, which can bind and activate GCN2 kinase to reduce translation. Here, we show that glutamine-specific tRNAs selectively become uncharged when extracellular amino acid availability is compromised. In contrast, all other tRNAs retain charging of their cognate amino acids in a manner that is dependent upon intact lysosomal function. In addition to GCN2 activation and reduced total translation, the reduced charging of tRNAGln in amino-acid-deprived cells also leads to specific depletion of proteins containing polyglutamine tracts including core-binding factor α1, mediator subunit 12, transcriptional coactivator CBP and TATA-box binding protein. Treating amino-acid-deprived cells with exogenous glutamine or glutaminase inhibitors restores tRNAGln charging and the levels of polyglutamine-containing proteins. Together, these results demonstrate that the activation of GCN2 and the translation of polyglutamine-encoding transcripts serve as key sensors of glutamine availability in mammalian cells.

| S-EPMC7744096 | biostudies-literature

Uncharged tRNAGln as an indicator of intracellular amino acid level upregulates UBC expression to maintain its charging level VI

Project description:We profiled the cellular tRNA charging landscape using next-generation sequencing and identified a subset of tRNA that sense nutrients. The charging levels of tRNAGln were exclusively and significantly decreased in response to amino acid starvation.

2022-11-30 | GSE188861 | GEO

Uncharged tRNAGln as an indicator of intracellular amino acid level upregulates UBC expression to maintain its charging level I

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Uncharged tRNAGln as an indicator of intracellular amino acid level upregulates UBC expression to maintain its charging level V

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Uncharged tRNAGln as an indicator of intracellular amino acid level upregulates UBC expression to maintain its charging level IV

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Uncharged tRNAGln as an indicator of intracellular amino acid level upregulates UBC expression to maintain its charging level III

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