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

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  • Chi-Kang Tseng

    (Howard Hughes Medical Institute
    Stowers Institute for Medical Research
    Institute of Developmental Biology and Neurobiology, Johannes Gutenberg University)

  • Hui-Fang Wang

    (Howard Hughes Medical Institute
    Stowers Institute for Medical Research
    Institute of Developmental Biology and Neurobiology, Johannes Gutenberg University)

  • Morgan R. Schroeder

    (Stowers Institute for Medical Research
    ArcherDX)

  • Peter Baumann

    (Howard Hughes Medical Institute
    Stowers Institute for Medical Research
    University of Kansas Medical Center
    Institute of Developmental Biology and Neurobiology, Johannes Gutenberg University)

Abstract

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.

Suggested Citation

  • Chi-Kang Tseng & Hui-Fang Wang & Morgan R. Schroeder & Peter Baumann, 2018. "The H/ACA complex disrupts triplex in hTR precursor to permit processing by RRP6 and PARN," Nature Communications, Nature, vol. 9(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-07822-6
    DOI: 10.1038/s41467-018-07822-6
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    Cited by:

    1. Jennifer Porat & Moaine El Baidouri & Jorg Grigull & Jean-Marc Deragon & Mark A. Bayfield, 2022. "The methyl phosphate capping enzyme Bmc1/Bin3 is a stable component of the fission yeast telomerase holoenzyme," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    2. Ross A. Cordiner & Yuhui Dou & Rune Thomsen & Andrii Bugai & Sander Granneman & Torben Heick Jensen, 2023. "Temporal-iCLIP captures co-transcriptional RNA-protein interactions," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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