ArticleBiology open2016
The decapping activator Edc3 and the Q/N-rich domain of Lsm4 function together to enhance mRNA stability and alter mRNA decay pathway dependence in Saccharomyces cerevisiae.
Article in Biology open, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Growth-regulated co-occupancy of Mediator and Lsm3 at intronic ribosomal protein genes.Nucleic acids research · 2024Article
- Arginine methylation of SM-LIKE PROTEIN 4 antagonistically affects alternative splicing during Arabidopsis stress responses.The Plant cell · 2024Article
- A distinct P-body-like granule is induced in response to the disruption of microtubule integrity in Saccharomyces cerevisiae.Genetics · 2022Article
- Post-transcriptional regulation during stress.FEMS yeast research · 2022Review
- Global SLAM-seq for accurate mRNA decay determination and identification of NMD targets.RNA (New York, N.Y.) · 2022Article
- Article
- P38 activation induces the dissociation of tristetraprolin from Argonaute 2 to increase ARE-mRNA stabilization.Molecular biology of the cell · 2018Article
- Recognition of RNA NNature cell biology · 2018Article
- An mRNA decapping mutant deficient in P body assembly limits mRNA stabilization in response to osmotic stress.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The rate and regulation of mRNA decay are major elements in the proper control of gene expression. Edc3 and Lsm4 are two decapping activator proteins that have previously been shown to function in the assembly of RNA granules termed P bodies. Here, we show that deletion of edc3, when combined with a removal of the glutamine/asparagine rich region of Lsm4 (edc3Δ lsm4ΔC) reduces mRNA stability and alters pathways of mRNA degradation. Multiple tested mRNAs exhibited reduced stability in the edc3Δ lsm4ΔC mutant. The destabilization was linked to an increased dependence on Ccr4-mediated deadenylation and mRNA decapping. Unlike characterized mutations in decapping factors that either are neutral or are able to stabilize mRNA, the combined edc3Δ lsm4ΔC mutant reduced mRNA stability. We characterized the growth and activity of the major mRNA decay systems and translation in double mutant and wild-type yeast. In the edc3Δ lsm4ΔC mutant, we observed alterations in the levels of specific mRNA decay factors as well as nuclear accumulation of the catalytic subunit of the decapping enzyme Dcp2. Hence, we suggest that the effects on mRNA stability in the edc3Δ lsm4ΔC mutant may originate from mRNA decay protein abundance or changes in mRNPs, or alternatively may imply a role for P bodies in mRNA stabilization.
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