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

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 which is distinct from th...

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Autores principales: Qi, Xiaodong, Rand, Dustin P., Podlevsky, Joshua D., Li, Yang, Mosig, Axel, Stadler, Peter F., Chen, Julian J.-L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4299825/
https://www.ncbi.nlm.nih.gov/pubmed/25598218
http://dx.doi.org/10.1038/ncomms7105
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author Qi, Xiaodong
Rand, Dustin P.
Podlevsky, Joshua D.
Li, Yang
Mosig, Axel
Stadler, Peter F.
Chen, Julian J.-L.
author_facet Qi, Xiaodong
Rand, Dustin P.
Podlevsky, Joshua D.
Li, Yang
Mosig, Axel
Stadler, Peter F.
Chen, Julian J.-L.
author_sort Qi, Xiaodong
collection PubMed
description 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 which 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.
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spelling pubmed-42998252015-07-19 Prevalent and distinct spliceosomal 3′-end processing mechanisms for fungal telomerase RNA Qi, Xiaodong Rand, Dustin P. Podlevsky, Joshua D. Li, Yang Mosig, Axel Stadler, Peter F. Chen, Julian J.-L. Nat Commun Article 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 which 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. 2015-01-19 /pmc/articles/PMC4299825/ /pubmed/25598218 http://dx.doi.org/10.1038/ncomms7105 Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Qi, Xiaodong
Rand, Dustin P.
Podlevsky, Joshua D.
Li, Yang
Mosig, Axel
Stadler, Peter F.
Chen, Julian J.-L.
Prevalent and distinct spliceosomal 3′-end processing mechanisms for fungal telomerase RNA
title Prevalent and distinct spliceosomal 3′-end processing mechanisms for fungal telomerase RNA
title_full Prevalent and distinct spliceosomal 3′-end processing mechanisms for fungal telomerase RNA
title_fullStr Prevalent and distinct spliceosomal 3′-end processing mechanisms for fungal telomerase RNA
title_full_unstemmed Prevalent and distinct spliceosomal 3′-end processing mechanisms for fungal telomerase RNA
title_short Prevalent and distinct spliceosomal 3′-end processing mechanisms for fungal telomerase RNA
title_sort prevalent and distinct spliceosomal 3′-end processing mechanisms for fungal telomerase rna
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4299825/
https://www.ncbi.nlm.nih.gov/pubmed/25598218
http://dx.doi.org/10.1038/ncomms7105
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