Abstract
Tudor staphylococcal nucleases (TSNs) are evolutionarily conserved RNA binding proteins, which include redundant TSN1 and TSN2 in Arabidopsis. It has been showed TSNs are the components of stress granules (SGs) and regulate plant growth under salt stress. In this study, we find a binding protein of TSN1, RH31, which is a DEAD-box RNA helicase (RH). Subcellular localization studies show that RH31 is mainly located in the nucleus, but under salinity, it translocates to the cytoplasm where it accumulates in cytoplasmic granules. After cycloheximide (CHX) treatment which can block the formation of SGs by interfering with mRNP homeostasis, these cytoplasmic granules disappeared. More importantly, RH31 co-localizes with SGs marker protein RBP47. RH31 deletion results in salt-hypersensitive phenotype, while RH31 overexpression causes more resistant to salt stress. In summary, we demonstrate that RH31, the TSN1 binding protein, is a component of plant SGs and participates in regulation of salt-stress tolerance in Arabidopsis.
Highlights
Abiotic stresses affect plant normal growth and lead to crop losses
Tudor staphylococcal nucleases (TSNs) is established with an important role in stress signaling as a docking platform for stress granule proteins (GutierrezBeltran et al, 2021)
We identified a binding protein of TSN1, RH31 (Aubourg et al, 1999), which belongs to the DEAD-box RNA helicase (RH) family
Summary
Abiotic stresses affect plant normal growth and lead to crop losses. Plants resist these environmental stresses by regulating mRNA translation and protein synthesis to alter the proteome rapidly in response to various stress signals. Stress granules (SGs) formation is thought to be required for the post-transcriptional regulation of stress-responsive mRNAs (Tsai et al, 2017; Omer et al, 2018). SGs are condensates of proteins and RNAs assembled via liquid–liquid phase separation which involvement plays emerging roles in RNA-related cellular events under various stresses (Ivanov et al, 2019; Lin and Fang, 2021). SGs function in the mammalian stress response by sequestering mRNAs and allowing for dynamic sorting of mRNAs for translation, storage, or degradation (Vanderweyde et al, 2013).
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