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

Xiaodong Qi, Dustin P. Rand, Joshua D. Podlevsky, Yang Li, Axel Mosig, Peter F. Stadler and Julian J. -L. Chen ()
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Xiaodong Qi: Arizona State University
Dustin P. Rand: Arizona State University
Joshua D. Podlevsky: Arizona State University
Yang Li: Arizona State University
Axel Mosig: Ruhr-University Bochum
Peter F. Stadler: and Interdisciplinary Center for Bioinformatics, University of Leipzig
Julian J. -L. Chen: Arizona State University

Nature Communications, 2015, vol. 6, issue 1, 1-8

Abstract: 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.

Date: 2015
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DOI: 10.1038/ncomms7105

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