Abstract

The Tudor-SN protein (TSN) is universally expressed and highly conserved in eukaryotes. In Arabidopsis, TSN is reportedly involved in stress adaptation, but the mechanism involved in this adaptation is not understood. Here, we provide evidence that TSN regulates the mRNA levels of GA20ox3, a key enzyme for gibberellin (GA) biosynthesis. The levels of GA20ox3 transcripts decreased in TSN1/TSN2 RNA interference (RNAi) transgenic lines and increased in TSN1 over-expression (OE) transgenic lines. The TSN1 OE lines displayed phenotypes that may be attributed to the overproduction of GA. No obvious defects were observed in the RNAi transgenic lines under normal conditions, but under salt stress conditions these lines displayed slower growth than wild-type (WT) plants. Two mutants of GA20ox3, ga20ox3-1 and -2, also showed slower growth under stress than WT plants. Moreover, a higher accumulation of GA20ox3 transcripts was observed under salt stress. The results of a western blot analysis indicated that higher levels of TSN1 accumulated after salt treatment than under normal conditions. Subcellular localization studies showed that TSN1 was uniformly distributed in the cytoplasm under normal conditions but accumulated in small granules and co-localized with RBP47, a marker protein for stress granules (SGs), in response to salt stress. The results of RNA immunoprecipitation experiments indicated that TSN1 bound GA20ox3 mRNA in vivo. On the basis of these findings, we conclude that TSN is a novel component of plant SGs that regulates growth under salt stress by modulating levels of GA20ox3 mRNA.

Highlights

  • The Tudor-SN protein (TSN) is universally expressed and highly conserved in eukaryotes

  • We found that the mRNA levels of GA20ox3, which encodes a key enzyme for GA biosynthesis, were decreased in a tsn1 mutant (Liu et al, 2010)

  • Our previous study showed that the mRNA levels of GA20ox3, which encodes a key enzyme for GA biosynthesis, was decreased in a TSN1 T-DNA insertion mutant (Liu et al, 2010)

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Summary

Introduction

The Tudor-SN protein (TSN) is universally expressed and highly conserved in eukaryotes. It possesses four complete N-terminal staphylococcal nuclease (SNc) domains, a central Tudor domain, and a partial SNc domain at the C-terminus. Gao et al (2010) reported that TSN interacts and co-localizes with G3BP in stress granules (SGs) under stress conditions in animals. TSN binds a variety of RNAs, including prolamine RNA, and associates with the cytoskeleton by interacting with other proteins (Sami-Subbu et al, 2001). Subsequent studies have shown that TSN participates in the localization of prolamine mRNAs in rice endosperm (Wang et al, 2008).

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