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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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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.

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Maturation of human telomerase RNA component from an extended precursor

Project description:Here, we develop nascent RNAend-Seq, in which we isolate nascent RNA and sequence the 3' ends of RNA precursors. Using a pulse-chase experimental design, we follow extended precursors of the telomerase RNA component (hTR) and show that the mature telomerase RNA derives from these species with slow kinetics compared to other small non-coding RNAs. The human disease causing gene PARN further delays maturation of the hTR precursor in PARN- mutant cancer cell lines. Disruption of the poly(A)polymerase PAPD5 in PARN-mutant cells restores normal processing kinetics and levels of mature hTR. Unexpectedly, neither PARN nor PAPD5 is required for hTR processing. Instead, PAPD5 and PARN set the hTR maturation rate by controlling precursor adenylation.

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2007-04-23 | GSE7136 | GEO

Genome-scale methylome profiling of adrenocortical carcinomas (ACC) and adenomas (ACA)

Project description:Genome-scale DNA methylation was analyzed in a cohort of ACC and ACA to identify DNA methylation changes. Bisulfite converted DNA from 51 fresh frozen ACC and 30 ACA samples were hybridized to Illumina HumanMethylation27 BeadChips.

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Next generation sequencing identifies polyadenylated species of hTR

Project description:The paired-end next-generation sequencing of all hTR versions of less than 200 nucleotides in length was used to analyze the 3’ end distribution of hTR associated to Flag-tagged versions of PABPN1, hTERT and Dyskerin. In total, we obtained 2,716,342, 3,152,013, and 3,077,395 hTR-specific reads for the PABPN1, hTERT, and Dyskerin purifications, respectively. We found that the majority of polyadenylated telomerase RNA recovered in the PABPN1, hTERT, and Dyskerin purifications had poly(A) tails starting immediately after the annotated hTR 3’ end. However, a greater proportion of poly(A) tails were found on genome-encoded 3’-extentions in the PABPN1-bound fraction compared to the population of hTR that was copurified with hTERT and DKC1: 15.5% for PABPN1, 6.9% for hTERT, and 6.5% for Dyskerin. Notably, the population of polyadenylated telomerase RNA recovered with PABPN1 was significantly different in terms of poly(A) tail length compared to polyadenylated hTR retrieved in the hTERT- and Dyskerin-bound fractions (P-value=5.551e-16, Kolmogorov-Smirnov test), showing a tendency toward longer poly(A) tails in the PABPN1-bound fraction. The enrichment of telomerase RNA with long poly(A) tails in the PABPN1-bound fraction is consistent with a role of PABPN1 in a maturation pathway that depends on hTR 3’ end polyadenylation. Moreover, our results indicate that a fraction of hTERT and Dyskerin are associated with polyadenylated versions of hTR.

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2019-01-15 | GSE125024 | GEO

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