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Angel2 phosphatase activity is required for non-canonical mitochondrial RNA processing in metazoa

ABSTRACT: Angel2 phosphatase activity is required for non-canonical mitochondrial RNA processing in metazoa

PROVIDER: PRJNA784409 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR17062619_1.fastq.gz	Fastqsanger.gz
	SRR17062619_2.fastq.gz	Fastqsanger.gz
	SRR17062620_1.fastq.gz	Fastqsanger.gz
	SRR17062620_2.fastq.gz	Fastqsanger.gz
	SRR17062621_1.fastq.gz	Fastqsanger.gz

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Angel2 phosphatase activity is required for non-canonical mitochondrial RNA processing in metazoa

Project description:Canonical RNA processing in mammalian mitochondria necessitates that tRNAs are recognised by nucleases to release flanking transcripts. However, not all mitochondrial transcripts are punctuated by tRNAs, and the mechanism and factors involved in their processing has remained unsolved. Here, we demonstrate that phosphatase activity of the carbon catabolite repressor 4 domain containing family member ANGEL2 is required for the hydrolysis of 3′ phosphates, resulting from non-canonical processing. Interaction studies in Drosophila further identify that members of the FAST kinase domain containing protein family are involved in the formation of these 3′ phosphates. Our results therefore resolve the mechanism of RNA processing in metazoan mitochondria, by defining the outstanding non-canonical processing mechanism.

2022-09-04 | GSE189750 | GEO

Angel2 phosphatase activity is required for non-canonical mitochondrial RNA processing

Project description:Canonical RNA processing in mammalian mitochondria is defined by tRNAs acting as recognition sites for nucleases to release flanking transcripts. The relevant factors, their structures, and mechanism are well described, but not all mitochondrial transcripts are punctuated by tRNAs, and their mode of processing has remained unsolved. Using Drosophila and mouse models, we demonstrate that non-canonical processing results in the formation of 3′ phosphates, and that phosphatase activity by the carbon catabolite repressor 4 domain-containing family member ANGEL2 is required for their hydrolysis. Furthermore, our data suggest that members of the FAST kinase domain-containing protein family are responsible for these 3′ phosphates. Our results therefore resolve the mechanism of non-canonical RNA processing in metazoan mitochondria, by defining the role of ANGEL2.

2022-09-01 | PXD033394 | Pride

ANGEL2 phosphatase activity is required for non-canonical mitochondrial RNA processing.

Project description:Canonical RNA processing in mammalian mitochondria is defined by tRNAs acting as recognition sites for nucleases to release flanking transcripts. The relevant factors, their structures, and mechanism are well described, but not all mitochondrial transcripts are punctuated by tRNAs, and their mode of processing has remained unsolved. Using Drosophila and mouse models, we demonstrate that non-canonical processing results in the formation of 3' phosphates, and that phosphatase activity by the carbon catabolite repressor 4 domain-containing family member ANGEL2 is required for their hydrolysis. Furthermore, our data suggest that members of the FAST kinase domain-containing protein family are responsible for these 3' phosphates. Our results therefore propose a mechanism for non-canonical RNA processing in metazoan mitochondria, by identifying the role of ANGEL2.

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The Protein Phosphatase 4 Complex Promotes Transcription and Processing of Primary microRNAs in Arabidopsis [ncRNA-Seq]

Project description:Protein phosphatase 4 (PP4) is a highly conserved serine/threonine protein phosphatase in yeast, plants, and animals. The composition and functions of the plant PP4 are poorly understood. Here, we uncovered previously unsuspected complexity of Arabidopsis PP4 and identified the composition of one form of PP4 containing the regulatory subunit PP4R3A. We showed that PP4R3A, together with one of two redundant catalytic subunit genes PPX1 and PPX2, promotes the biogenesis of microRNAs. PP4R3A is a chromatin-associated protein, interacts with RNA polymerase II (Pol II), and recruits Pol II to the promoters of MIR genes to promote their transcription. PP4R3A probably also promotes the cotranscriptional processing of miRNA precursors as it recruits the microprocessor component HYPONASTIC LEAVES1 (HYL1) to MIR genes and nuclear dicing bodies. Moreover, we showed that hundreds of introns exhibit splicing defects in pp4r3a mutants. Together, this study revealed a role of Arabidopsis PP4 in transcription and nuclear RNA metabolism.

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The Protein Phosphatase 4 Complex Promotes Transcription and Processing of Primary microRNAs in Arabidopsis

Project description:The Protein Phosphatase 4 Complex Promotes Transcription and Processing of Primary microRNAs in Arabidopsis

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