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Published on: November 8, 2006
Pan2-Pan3 complex, together with Ccr4-Not complex, has a role in the cell growth on non-fermentable carbon sources
Shiori Fujii1, Duong Long Duy1, Arvin Lapiz Valderrama2
1Department of Molecular Cell Biology, Graduate School of Comprehensive Human Sciences and Faculty of Medicine, University of Tsukuba, Tsukuba, Japan.
Abstract:
There are two major deadenylase complexes, Ccr4-Not and Pan2-Pan3, which shorten the 3' poly(A) tail of mRNA and are conserved from yeast to human. We have previously shown that the Ccr4-mediated deadenylation plays the important role in gene expression regulation in the yeast stationary phase cell. In order to further understand the role of deadenylases in different growth condition, in this study we investigated the effect of deletion of both deadenylases on the cell in non-fermentable carbon containing media. We found that both ccr4Δ and ccr4Δ pan2Δ mutants showed similar growth defect in YPD media: when switched to media containing non-fermentable source (Glycerol-Lactate) only the ccr4Δ grew while the ccr4Δ pan2Δ did not. Ccr4, Pan2, and Pan3 were phosphorylated in GlyLac medium, suggesting that the activities of Ccr4, Pan2, and Pan3 may be regulated by phosphorylation in response to change of carbon sources. To get insights how Ccr4 and Pan2 function in the cell growth in media containing non-fermentable source only, we isolated multicopy suppressors for the growth defect on YPGlyLac media of the ccr4Δ pan2Δ mutant and identified two genes, STM1 and REX2, which encode a ribosome-associated protein and a 3'-5' RNA exonuclease, respectively. Our results suggest that the Pan2-Pan3 complex, together with the Ccr4-Not complex, has important roles in the growth on non-fermentable carbon sources.
Insights
Investigating yeast deadenylases Ccr4-Not and Pan2-Pan3 in non-fermentable media revealed distinct roles. Deleting both complexes caused severe growth defects, suggesting their crucial involvement in utilizing alternative carbon sources.
Area of Science:
- * Molecular Biology
- * Genetics
- * Yeast Biology
Background:
- * Two major mRNA deadenylase complexes, Ccr4-Not and Pan2-Pan3, regulate gene expression by shortening the poly(A) tail.
- * Ccr4-mediated deadenylation is crucial for gene expression in yeast stationary phase.
- * The roles of these deadenylases in different growth conditions, particularly with non-fermentable carbon sources, require further investigation.
Purpose of the Study:
- * To investigate the impact of deleting both Ccr4-Not and Pan2-Pan3 deadenylase complexes on yeast cell growth in non-fermentable media.
- * To understand the regulatory mechanisms, such as phosphorylation, of these deadenylases under varying carbon source conditions.
- * To identify genes that can suppress growth defects associated with the loss of deadenylase function in non-fermentable media.
Main Methods:
- * Comparative growth analysis of wild-type, ccr4Δ, and ccr4Δ pan2Δ yeast mutants in YPD and Glycerol-Lactate (GlyLac) media.
- * Phosphorylation analysis of Ccr4, Pan2, and Pan3 proteins in GlyLac medium.
- * Genetic screening for multicopy suppressors of the ccr4Δ pan2Δ growth defect on YPGlyLac.
Main Results:
- * While ccr4Δ mutants showed a growth defect in YPD, ccr4Δ pan2Δ mutants exhibited a similar defect. Upon switching to GlyLac medium, only ccr4Δ grew, while ccr4Δ pan2Δ did not.
- * Ccr4, Pan2, and Pan3 proteins were found to be phosphorylated in GlyLac medium, suggesting post-translational regulation in response to carbon source.
- * Multicopy suppressors STM1 and REX2 were identified for the ccr4Δ pan2Δ growth defect, encoding a ribosome-associated protein and an RNA exonuclease, respectively.
Conclusions:
- * The Pan2-Pan3 complex, in addition to the Ccr4-Not complex, plays a significant role in yeast growth on non-fermentable carbon sources.
- * Phosphorylation likely serves as a regulatory mechanism for deadenylase activity in response to environmental cues like carbon source availability.
- * The identification of STM1 and REX2 provides insights into cellular pathways that compensate for deadenylase loss during growth on non-fermentable substrates.
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