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The H/ACA complex disrupts triplex in hTR precursor to permit processing by RRP6 and PARN

ABSTRACT: The H/ACA complex disrupts triplex in hTR precursor to permit processing by RRP6 and PARN

PROVIDER: PRJNA435870 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR6781094.fastq.gz	Fastqsanger.gz
	SRR6781095.fastq.gz	Fastqsanger.gz
	SRR6781096.fastq.gz	Fastqsanger.gz
	SRR6781097.fastq.gz	Fastqsanger.gz
	SRR6781098.fastq.gz	Fastqsanger.gz

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The H/ACA complex disrupts triplex in hTR precursor to permit processing by RRP6 and PARN

Project description:Human telomerase RNA (hTR) is transcribed as a precursor that is then posttranscriptionally modified and processed. A fraction of the transcripts is oligoadenylated by TRAMP and either processed into the mature hTR or degraded by the exosome. Here, we characterize the processing of 3’ extended forms of varying length by PARN and RRP6. We show that tertiary RNA interactions unique to the longer precursor forms favor RNA degradation, whereas H/ACA RNP assembly stimulates productive processing. Interestingly, the H/ACA complex actively promotes processing in addition to protecting the mature 3’ end. Processing occurs in two steps with longer forms being trimmed by RRP6 and shorter forms being preferentially processed by PARN. These results reveal how RNA structure and RNP assembly affect the kinetics of processing and degradation and ultimately determine the amount of functional telomerase produced in cells.

2018-12-26 | GSE111081 | GEO

The H/ACA complex disrupts triplex in hTR precursor to permit processing by RRP6 and PARN.

Project description:Human telomerase RNA (hTR) is transcribed as a precursor that is then posttranscriptionally modified and processed. A fraction of the transcripts is oligoadenylated by TRAMP and either processed into the mature hTR or degraded by the exosome. Here, we characterize the processing of 3' extended forms of varying length by PARN and RRP6. We show that tertiary RNA interactions unique to the longer transcripts favor RNA degradation, whereas H/ACA RNP assembly stimulates productive processing. Interestingly, the H/ACA complex actively promotes processing in addition to protecting the mature 3' end. Processing occurs in two steps with longer forms first being trimmed by RRP6 and shorter forms then being processed by PARN. These results reveal how RNA structure and RNP assembly affect the kinetics of processing and degradation and ultimately determine the amount of functional telomerase produced in cells.

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PARN and TOE1 constitute a 3′ end maturation module for nuclear non-coding RNAs

Project description:Poly(A)-specific ribonuclease (PARN) and target of EGR1 protein 1 (TOE1) are nuclear granule-associated deadenylases, whose mutations are linked to multiple human diseases. Here, we applied mTAIL-seq and RNA sequencing (RNA-seq) to systematically identify the substrates of PARN and TOE1 and elucidate their molecular functions. We found that PARN and TOE1 do not modulate the length of mRNA poly(A) tails. Rather, they promote the maturation of nuclear small non-coding RNAs (ncRNAs). PARN and TOE1 act redundantly on some ncRNAs, most prominently small Cajal body-specific RNAs (scaRNAs). scaRNAs are strongly downregulated when PARN and TOE1 are compromised together, leading to defects in small nuclear RNA (snRNA) pseudouridylation. They also function redundantly in the biogenesis of telomerase RNA component (TERC), which shares sequence motifs found in H/ACA box scaRNAs. Our findings extend the knowledge of nuclear ncRNA biogenesis, and they provide insights into the pathology of PARN/TOE1-associated genetic disorders whose therapeutic treatments are currently unavailable.

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