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N1-methyladenosine modification in mitochondrial tRNAs is associated with Alzheimer’s disease

ABSTRACT: N1-methyladenosine modification in mitochondrial tRNAs is associated with Alzheimer’s disease

PROVIDER: PRJNA706440 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR18572710.fastq.gz	Fastqsanger.gz
	SRR18572711.fastq.gz	Fastqsanger.gz
	SRR18572712.fastq.gz	Fastqsanger.gz
	SRR18572713.fastq.gz	Fastqsanger.gz
	SRR18572714.fastq.gz	Fastqsanger.gz

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N1-methyladenosine modification in mitochondrial tRNAs is associated with Alzheimer’s disease

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tRNA modification landscape selectively controls mitochondrial translation efficiency in MERRF

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Prokaryotic N1-methyladenosine erasers maintain tRNA m1A modification levels in Streptomyces venezuelae.

Project description:Prokaryotic N1-methyladenosine erasers maintain tRNA m1A modification levels in Streptomyces venezuelae.

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Transcriptome-wide mapping reveals reversible and dynamic N1-methyladenosine methylome

Project description:N1-Methyladenosine (m1A) is a prevalent post-transcriptional RNA modification, yet little is known about its abundance, topol- ogy and dynamics in mRNA. Here, we show that m1A is prevalent in Homo sapiens mRNA, which shows an m1A/A ratio of ~0.02%. We develop the m1A-ID-seq technique, based on m1A immunoprecipitation and the inherent ability of m1A to stall reverse tran- scription, as a means for transcriptome-wide m1A profiling. m1A-ID-seq identifies 901 m1A peaks (from 600 genes) in mRNA and noncoding RNA and reveals a prominent feature, enrichment in the 5' untranslated region of mRNA transcripts, that is dis- tinct from the pattern for N6-methyladenosine, the most abundant internal mammalian mRNA modification. Moreover, m1A in mRNA is reversible by ALKBH3, a known DNA/RNA demethylase. Lastly, we show that m1A methylation responds dynamically to stimuli, and we identify hundreds of stress-induced m1A sites. Collectively, our approaches allow comprehensive analysis of m1A modification and provide tools for functional studies of potential epigenetic regulation via the reversible and dynamic m1A methylation.

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Queuosine modification protects cognate tRNAs against ribonuclease cleavage

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