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UPF1 helicase promotes Tudor-SN-mediated miRNA decay

ABSTRACT: The helicase activity of UPF1 remodels miRNPs so as to render miRNAs susceptible to Tudor-SN (TSN)-mediated miRNA decay

ORGANISM(S): Homo sapiens

PROVIDER: GSE100068 | GEO | 2017/08/22

SECONDARY ACCESSION(S): PRJNA390626

REPOSITORIES: GEO

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Gene expression in Tudor-SN knockdown Drosophila in normoxic and hypoxic conditions

Project description:The RNA-binding protein Snd1/Tudor-SN can regulate gene expression through various mechanisms and is suggested to function in stress responses. Here we have analyzed mRNA expression in Tudor-SN knockdown and control flies in hypoxic and normoxic conditions.

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Project description:One OsTudor-SN mutant, EM1084, carrying E503K point mutation and one associated WT-OsTSN complemented transgenic (pHL8042/EM1084 ) were applied in this study. EM1084 was obtained by TILLING studies (http://www.shigen.nig.ac.jp/rice/oryzabase). The E503K mutation site in EM1084 lies within the SN3 domain, while the EM1084 complemented transgenic plant was complemented with the full-length WT OsTSN gene driven by native OsTSN promoter. This mutation results in affecting storage protein mRNA localization and, in turn, with a strong reduction in grain weight and storage protein accumulation. Transcriptome analysis on the dehulled 10-14 days old developing seeds from wild type, EM1084 and pHL8042/EM1084 indicates that partial loss of Tudor-SN function caused the differential expression of storage protein genes and relevant genes involved in several essential biological processes during rice development.

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Project description:Tudor staphylococcal nuclease (TSN or Tudor-SN; also known as SND1) is an evolutionarily conserved protein involved in transcriptional and post-transcriptional regulation of gene expression in animals. Although TSN was found to be indispensable for normal plant development and stress tolerance, the molecular mechanisms underlying these functions remain elusive. Here we show that Arabidopsis thaliana TSN is essential for integrity and function of cytoplasmic messenger ribonucleoprotein (mRNP) complexes called stress granules (SG) and processing bodies (PB), sites of post-transcriptional gene regulation during stress. TSN associates with SG following their microtubule-dependent assembly and plays a scaffolding role in both SG and PB. The enzymatically active tandem repeat of four SN domains is crucial for targeting TSN to the cytoplasmic mRNA complexes, and is sufficient for the cytoprotective function of TSN during stress. Furthermore, our work connects the cytoprotective function of TSN with its positive role in stress-induced mRNA decapping. While stress led to a pronounced increase in the accumulation of uncapped mRNAs in wild type plants, this increase was abrogated in TSN knockout plants. Taken together, our results establish TSN as a key enzymatic component of catabolic machinery responsible for the processing of mRNAs in the cytoplasmic mRNP complexes during stress.

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Homo sapiens

Project description:UPF1 helicase promotes Tudor-SN-mediated miRNA decay

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