An RNA‐binding protein homologue that promotes sporulation‐specific gene expression in Saccharomyces cerevisiae

Prior studies have shown that S. cerevisiae rim4 mutations cause reduced expression of a sporulation‐specific reporter gene and sporulation. We report here that RIM4 (ORF YHL024W) is a putative RNA‐binding protein of the RRM class that is expressed at elevated levels early in meiosis. Mutations in t...

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Bibliographic Details
Published in:Yeast (Chichester, England) England), 2000-05, Vol.16 (7), p.631-639
Main Authors: Soushko, Maria, Mitchell, Aaron P.
Format: Article
Language:English
Subjects:
Cell Cycle Proteins
dyads
Fungal Proteins - genetics
Fungal Proteins - metabolism
Gene Expression Regulation, Fungal
Ime1 protein
Ime2 protein
Intracellular Signaling Peptides and Proteins
Meiosis
Protein Kinases - genetics
Protein Kinases - metabolism
Protein-Serine-Threonine Kinases
RIM4 gene
RIM4 protein
Rim4p protein
RNA-Binding Proteins - genetics
RNA-Binding Proteins - metabolism
RNA‐binding protein
Saccharomyces cerevisiae
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae - physiology
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
Spores, Fungal - genetics
Spores, Fungal - physiology
sporulation
Transcription, Genetic
Transcriptional Activation
transcriptional regulation
YHL024W gene
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Summary:Prior studies have shown that S. cerevisiae rim4 mutations cause reduced expression of a sporulation‐specific reporter gene and sporulation. We report here that RIM4 (ORF YHL024W) is a putative RNA‐binding protein of the RRM class that is expressed at elevated levels early in meiosis. Mutations in the two RRMs reduce or abolish sporulation and, in some cases, cause reduced Rim4p expression. RIM4 is required for expression of early and middle sporulation‐specific genes. Unlike other meiotic regulatory genes, RIM4 is required for full gene activation through both the Ime1p and Ime2p pathways. The rim4Δ defect in activation by Ime2p is suppressed by a hyperactive Ime2p derivative. These observations argue that Rim4p may act upstream of Ime2p, perhaps in a nutritional sensing pathway. Copyright © 2000 John Wiley & Sons, Ltd.
ISSN:0749-503X
1097-0061
DOI:10.1002/(SICI)1097-0061(200005)16:7<631::AID-YEA559>3.0.CO;2-U