An essential role for trimethylguanosine RNA caps in Saccharomyces cerevisiae meiosis and their requirement for splicing of SAE3 and PCH2 meiotic pre-mRNAs Journal Article

   

Authors:	Qiu, Z. R.; Shuman, S.; Schwer, B.
Article Title:	An essential role for trimethylguanosine RNA caps in Saccharomyces cerevisiae meiosis and their requirement for splicing of SAE3 and PCH2 meiotic pre-mRNAs
Abstract:	Tgs1 is the enzyme that converts m7G RNA caps to the 2,2,7-trimethylguanosine (TMG) caps characteristic of spliceosomal snRNAs. Fungi grow vegetatively without TMG caps, thereby raising the question of what cellular transactions, if any, are TMG cap-dependent. Here, we report that Saccharomyces cerevisiae Tgs1 methyltransferase activity is essential for meiosis. tgs1Δ cells are specifically defective in splicing PCH2 and SAE3 meiotic pre-mRNAs. The TMG requirement for SAE3 splicing is alleviated by two intron mutations: a UAUUAAC to UACUAAC change that restores a consensus branchpoint and disruption of a stem-loop encompassing the branchpoint. The TMG requirement for PCH2 splicing is alleviated by a CACUAAC to UACUAAC change restoring a consensus branchpoint and by shortening the PCH2 5′ exon. Placing the SAE3 and PCH2 introns within a HIS3 reporter confers Tgs1-dependent histidine prototrophy, signifying that the respective introns are portable determinants of TMG-dependent gene expression. Analysis of in vitro splicing in extracts of TGS1 versus tgs1Δ cells showed that SAE3 intron removal was enfeebled without TMG caps, whereas splicing of ACT1 was unaffected. Our findings illuminate a new mode of tunable splicing, a reliance on TMG caps for an essential developmental RNA transaction, and three genetically distinct meiotic splicing regulons in budding yeast. © 2011 The Author(s).
Keywords:	controlled study; unclassified drug; gene mutation; exon; gene deletion; exons; nonhuman; genetic analysis; meiosis; gene expression; amino acid substitution; intron; introns; in vitro study; enzyme activity; nuclear proteins; rna-binding proteins; methyltransferase; methyltransferases; guanosine derivative; saccharomyces cerevisiae; guanosine; rna, messenger; reporter gene; saccharomyces cerevisiae proteins; saccharomycetales; nucleic acid conformation; protein secondary structure; fungi; histidine; rna splicing; rna precursors; messenger rna precursor; spores, fungal; adenine; uracil; cytosine; 2,2,7 trimethylguanosine; pch2 messenger rna precursor; sae3 messenger rna precursor; small nuclear rna; trimethylguanosine synthase 1; regulon; endonucleases
Journal Title:	Nucleic Acids Research
Volume:	39
Issue:	13
ISSN:	0305-1048
Publisher:	Oxford University Press
Date Published:	2011-07-01
Start Page:	5633
End Page:	5646
Language:	English
DOI:	10.1093/nar/gkr083
PROVIDER:	scopus
PMCID:	PMC3141232
PUBMED:	21398639
DOI/URL:	http://www.scopus.com/inward/record.url?eid=2-s2.0-80051832804&partnerID=40&md5=db49098a68c5c7db7bceffd81162868b
Notes:	--- - "Export Date: 3 October 2011" - "CODEN: NARHA" - "Source: Scopus"

https://synapse.mskcc.org/synapse/works/has_related_data_chk/13103