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Prevalent and distinct spliceosomal 3′-end processing mechanisms for fungal telomerase RNA

Author

Listed:
  • Xiaodong Qi

    (Arizona State University)

  • Dustin P. Rand

    (Arizona State University)

  • Joshua D. Podlevsky

    (Arizona State University)

  • Yang Li

    (Arizona State University
    Present address: Barrow Neurological Institute, Phoenix, Arizona 85013, USA)

  • Axel Mosig

    (Ruhr-University Bochum)

  • Peter F. Stadler

    (and Interdisciplinary Center for Bioinformatics, University of Leipzig)

  • Julian J. -L. Chen

    (Arizona State University)

Abstract

Telomerase RNA (TER) is an essential component of the telomerase ribonucleoprotein complex. The mechanism for TER 3′-end processing is highly divergent among different organisms. Here we report a unique spliceosome-mediated TER 3′-end cleavage mechanism in Neurospora crassa that is distinct from that found specifically in the fission yeast Schizosaccharomyces pombe. While the S. pombe TER intron contains the canonical 5′-splice site GUAUGU, the N. crassa TER intron contains a non-canonical 5′-splice site AUAAGU that alone prevents the second step of splicing and promotes spliceosomal cleavage. The unique N. crassa TER 5′-splice site sequence is evolutionarily conserved in TERs from Pezizomycotina and early branching Taphrinomycotina species. This suggests that the widespread and basal N. crassa-type spliceosomal cleavage mechanism is more ancestral than the S. pombe-type. The discovery of a prevalent, yet distinct, spliceosomal cleavage mechanism throughout diverse fungal clades furthers our understanding of TER evolution and non-coding RNA processing.

Suggested Citation

  • Xiaodong Qi & Dustin P. Rand & Joshua D. Podlevsky & Yang Li & Axel Mosig & Peter F. Stadler & Julian J. -L. Chen, 2015. "Prevalent and distinct spliceosomal 3′-end processing mechanisms for fungal telomerase RNA," Nature Communications, Nature, vol. 6(1), pages 1-8, May.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms7105
    DOI: 10.1038/ncomms7105
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