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Translational adaptation to heat stress is mediated by 5-methylcytosine RNA modification in Caenorhabditis elegans

ABSTRACT: Translational adaptation to heat stress is mediated by 5-methylcytosine RNA modification in Caenorhabditis elegans

PROVIDER: PRJNA605013 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR11031200_1.fastq.gz	Fastqsanger.gz
	SRR11031200_2.fastq.gz	Fastqsanger.gz
	SRR11031201_1.fastq.gz	Fastqsanger.gz
	SRR11031201_2.fastq.gz	Fastqsanger.gz
	SRR11031202_1.fastq.gz	Fastqsanger.gz

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Translational adaptation to heat stress is mediated by 5-methylcytosine RNA modification in Caenorhabditis elegans

Project description:Translational adaptation to heat stress is mediated by 5-methylcytosine RNA modification in Caenorhabditis elegans

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Translational adaptation to heat stress is mediated by 5-methylcytosine RNA modification in Caenorhabditis elegans

Project description:In order to fulfil a wide range of cellular functions, RNA molecules contain, in addition to the four canonical bases, a large number of chemically modified structures. Among those, the methylation of carbon-5 of cytosines (m5C) is an abundant, widespread mark in different classes of RNAs. m5C is catalysed by DNMT2 and by seven members of the NSUN family of enzymes. While some m5C-methyltransferases have been studied individually and implicated in phenotypes observed in organisms ranging from yeast to humans, it remains unclear how the m5C methylome acts to sustain development in homeostasis and stress. Here, using Caenorhabditis elegans as a model organism, we developed the first organism devoid of detectable m5C in RNA, providing strong evidence that this modification and its derivatives are non-essential for the nematode’s development and fertility under standard laboratory conditions. We further used this genetic tool to determine the localisation of m5C sites in different RNA classes, and showed that NSUN-4 acts as a multisite-specific tRNA/rRNA methyltransferase in the mitochondria. In addition, we show that m5C is required for adaptation to temperature changes, as animals devoid of this modification present temperature-sensitive fertility defects. At the molecular level, we show that loss of m5C leads to increased ribosome pausing at triplets encoding for leucine and proline, the most frequently methylated tRNA isoacceptors in C. elegans. This is correlated with reduced translation efficiency of transcripts enriched in these amino acids. Finally, we found translation of Leu-UUG codons to be the most strongly affected upon heat shock, suggesting a role of m5C wobble methylation in the adaptation to heat stress.

2020-11-06 | GSE144822 | GEO

Translational adaptation to heat stress is mediated by 5-methylcytosine RNA modification in Caenorhabditis elegans

2020-06-30 | GSE146256 | GEO

OsNSUN2-mediated 5-methylcytidine mRNA modification enhances rice adaptation to high-temperature

Project description:Heat stress is one of the extreme weather disasters potently decreasing cereal plant production. Recent studies have demonstrated that protein degradation and rRNA homeostasis as well as transcription factors are involved in thermoresponse in plants. However, how 5-methylcytosine (m5C) RNA modification contribute to heat stress response in plant remains largely unknown. Herein, we identified OsNSUN2 as the mRNA m5C methyltransferase in rice. The osnsun2 mutants specifically displayed severe phenotypes of temperature- and light-dependent lesion mimic and heat stress hypersensitivity. Heat stress enhanced mRNAs m5C methylation involving photosynthesis and detoxification systems, such as β-OsLCY, OsHO2, OsPAL1, and OsGLYI4, in an OsNSUN2-dependent manner, which then increased the protein synthesis. Consistently, the photosystem of the osnsun2 mutants was vulnerable to high ambient temperature and failed to be repaired under tolerable heat stress. Furthermore, OsNSUN2 mutation reduced photosynthesis efficiency and accumulated excessive reactive oxygen species upon heat treatment. Our findings demonstrate an important mechanism of mRNA m5C-dependent heat acclimation in rice.

2020-04-15 | PXD017187 | Pride

Translational adaptation to heat stress is mediated by RNA 5-methylcytosine in Caenorhabditis elegans.

Project description:Methylation of carbon-5 of cytosines (m5 C) is a post-transcriptional nucleotide modification of RNA found in all kingdoms of life. While individual m5 C-methyltransferases have been studied, the impact of the global cytosine-5 methylome on development, homeostasis and stress remains unknown. Here, using Caenorhabditis elegans, we generated the first organism devoid of m5 C in RNA, demonstrating that this modification is non-essential. Using this genetic tool, we determine the localisation and enzymatic specificity of m5 C sites in the RNome in vivo. We find that NSUN-4 acts as a dual rRNA and tRNA methyltransferase in C. elegans mitochondria. In agreement with leucine and proline being the most frequently methylated tRNA isoacceptors, loss of m5 C impacts the decoding of some triplets of these two amino acids, leading to reduced translation efficiency. Upon heat stress, m5 C loss leads to ribosome stalling at UUG triplets, the only codon translated by an m5 C34-modified tRNA. This leads to reduced translation efficiency of UUG-rich transcripts and impaired fertility, suggesting a role of m5 C tRNA wobble methylation in the adaptation to higher temperatures.

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Role of eEF2 diphthamide modification in translational fidelity

Project description:Role of eEF2 diphthamide modification in translational fidelity

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METTL8 is required for 3-methylcytosine modification in human mitochondrial tRNAs

Project description:A subset of eukaryotic tRNAs is methylated in the anticodon loop to form the 3-methylcytosine (m3C) modification. In mammals, the number of tRNAs containing m3C has expanded to include mitochondrial (mt) tRNA-Ser-UGA and mt-tRNA-Thr-UGU. Whereas the enzymes catalyzing m3C formation in nuclear-encoded cytoplasmic tRNAs have been identified, the proteins responsible for m3C modification in mt-tRNAs are unknown. Here, we show that m3C formation in human mt-tRNAs is dependent upon the Methyltransferase-Like 8 (METTL8) enzyme. We find that METTL8 is a mitochondria-associated protein that interacts with mitochondrial seryl-tRNA synthetase along with mt-tRNAs containing m3C. Human cells deficient in METTL8 exhibit loss of m3C modification in mt-tRNAs but not nuclear-encoded tRNAs. Consistent with the mitochondrial import of METTL8, the formation of m3C in METTL8-deficient cells can be rescued by re-expression of wildtype METTL8 but not by a METTL8 variant lacking the N-terminal mitochondrial localization signal. Notably, METTL8-deficiency in human cells causes alterations in the native migration pattern of mt-tRNA-Ser-UGA suggesting a role for m3C in tRNA folding. Altogether, these findings demonstrate that METTL8 is required for m3C formation in mitochondrial tRNAs and uncover a potential role for m3C modification in mitochondrial tRNA structure.

2022-05-19 | PXD030418 | Pride

5-methylcytosine modification and the ALYREF reader protein promote retrovirus replication

Project description:5-methylcytosine modification and the ALYREF reader protein promote retrovirus replication

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Comprehensive analysis of mRNA 5-methylcytosine modification in Eimeria tenella oocysts

Project description:Comprehensive analysis of mRNA 5-methylcytosine modification in Eimeria tenella oocysts

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Translational efficiency in mock- and heat-treated N.benthamiana leaves

Project description:Translational efficiency in mock- and heat-treated N.benthamiana leaves

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