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A subset of Mer1p-dependent introns requires Bud13p for splicing activation and nuclear retention.
RNA. 2006 Jul; 12(7):1361-72.RNA

Abstract

In the yeast Saccharomyces cerevisiae, Mer1p is expressed only during meiosis, and its expression is linked to the splicing of at least three mRNAs: MER2, MER3, and AMA1. Previous evidence suggests that Mer1p activates splicing by directly recruiting snRNPs or stabilizing intermediate splicing complexes formed on pre-mRNA that contains an intronic Mer1p enhancer element. However, some splicing factors, especially accessory/non-snRNP factors, have critical roles in retaining unspliced pre-mRNAs in the nucleus. We tested if Mer1p may indirectly regulate splicing by preventing the export of pre-mRNAs to the cytoplasm and also demonstrated that a second subunit of the Retention and Splicing (RES) complex, Bud13p, has transcript-specific effects on Mer1p-activated splicing. The results indicated that Mer1p can retain unspliced pre-mRNA in the nucleus; however, nuclear retention could not be uncoupled from splicing activation. In the absence of Mer1p, the AMA1 pre-mRNA is exported to the cytoplasm, translated, but not subjected to nonsense-mediated decay (NMD) despite a premature stop codon in the intron. These data imply that Mer1p can retain pre-mRNAs in the nucleus only by facilitating their interaction with the spliceosome and that two subunits of the RES complex modulate Mer1p function on two of the three Mer1p-dependent introns. The results also support models for cytoplasmic degradation of unspliced pre-mRNAs that fail to assemble into spliceosomes in yeast.

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Authors+Show Affiliations

Scherrer FW
Department of Biology, University of Missouri-St. Louis, MO 63121, USA.
Spingola M
No affiliation info available

MeSH

Cell NucleusIntronsMeiosisRNA PrecursorsRNA SplicingRNA, FungalRNA, MessengerRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteins

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16738408

Citation

Scherrer, Frederick W., and Marc Spingola. "A Subset of Mer1p-dependent Introns Requires Bud13p for Splicing Activation and Nuclear Retention." RNA (New York, N.Y.), vol. 12, no. 7, 2006, pp. 1361-72.
Scherrer FW, Spingola M. A subset of Mer1p-dependent introns requires Bud13p for splicing activation and nuclear retention. RNA. 2006;12(7):1361-72.
Scherrer, F. W., & Spingola, M. (2006). A subset of Mer1p-dependent introns requires Bud13p for splicing activation and nuclear retention. RNA (New York, N.Y.), 12(7), 1361-72.
Scherrer FW, Spingola M. A Subset of Mer1p-dependent Introns Requires Bud13p for Splicing Activation and Nuclear Retention. RNA. 2006;12(7):1361-72. PubMed PMID: 16738408.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A subset of Mer1p-dependent introns requires Bud13p for splicing activation and nuclear retention. AU - Scherrer,Frederick W,Jr AU - Spingola,Marc, Y1 - 2006/05/31/ PY - 2006/6/2/pubmed PY - 2006/8/15/medline PY - 2006/6/2/entrez SP - 1361 EP - 72 JF - RNA (New York, N.Y.) JO - RNA VL - 12 IS - 7 N2 - In the yeast Saccharomyces cerevisiae, Mer1p is expressed only during meiosis, and its expression is linked to the splicing of at least three mRNAs: MER2, MER3, and AMA1. Previous evidence suggests that Mer1p activates splicing by directly recruiting snRNPs or stabilizing intermediate splicing complexes formed on pre-mRNA that contains an intronic Mer1p enhancer element. However, some splicing factors, especially accessory/non-snRNP factors, have critical roles in retaining unspliced pre-mRNAs in the nucleus. We tested if Mer1p may indirectly regulate splicing by preventing the export of pre-mRNAs to the cytoplasm and also demonstrated that a second subunit of the Retention and Splicing (RES) complex, Bud13p, has transcript-specific effects on Mer1p-activated splicing. The results indicated that Mer1p can retain unspliced pre-mRNA in the nucleus; however, nuclear retention could not be uncoupled from splicing activation. In the absence of Mer1p, the AMA1 pre-mRNA is exported to the cytoplasm, translated, but not subjected to nonsense-mediated decay (NMD) despite a premature stop codon in the intron. These data imply that Mer1p can retain pre-mRNAs in the nucleus only by facilitating their interaction with the spliceosome and that two subunits of the RES complex modulate Mer1p function on two of the three Mer1p-dependent introns. The results also support models for cytoplasmic degradation of unspliced pre-mRNAs that fail to assemble into spliceosomes in yeast. SN - 1355-8382 UR - https://www.unboundmedicine.com/medline/citation/16738408/A_subset_of_Mer1p_dependent_introns_requires_Bud13p_for_splicing_activation_and_nuclear_retention_ DB - PRIME DP - Unbound Medicine ER -