Sodium Stress in the Halophyte Thellungiella halophila and Transcriptional Changes in a thsos1-RNA Interference Line

The plasma membrane Na＋/H＋-antiporter salt overly sensitive1 （SOS1） from the halophytic Arabidopsis-relative Thellungiella halophila （ThSOS1） shows conserved sequence and domain structure with the orthologous genes from Arabidopsis thaliana and other plants. When expression of ThSOSt was reduced by RNA interference （RNAi）, pronounced characteristics of salt-sensitivity were observed. We were interested in monitoring altered transcriptional responses between Thellungiella wild type and thsost-4, a representative RNAi line with particular emphasis on root responses to salt stress at 350 mmol/L NaCI, a concentration that is only moderately stressful for mature wild type plants. Transcript profiling revealed several functional categories of genes that were differently affected in wild-type and RNAi plants. Down-regulation of SOS1 resulted in different gene expression even in the absence of stress. The pattern of gene induction in the RNAi plant under salt stress was similar to that of glycophytic Arabidopsis rather than that of wild type Thellungiella. The RNAi plants failed to down-regulate functions that are normally reduced in wild type Thellungiella upon stress and did not up-regulate functions that characterize the Thellungiella salt stress response. Metabolite changes observed in wild type Thellungiella after salt stress were less pronounced or absent in RNAi plants. Transcript and metabolite behavior suggested SOS1 functions including but also extending its established function as a sodium transporter. The down-regulation of ThSOS1 converted the halophyte Thellungiella into a salt-sensitive plant.

The Asparagine-Rich Protein NRP Facilitates the Degradation of the PP6-type Phosphatase FyPP3 to Promote ABA Response in Arabidopsis

The phytohormone abscisic acid （ABA） plays critical roles in abiotic stress responses and plant develop- ment. In germinating seeds, the phytochrome-associated protein phosphatase, FyPP3, negatively regulates ABA signaling by dephosphorylating the transcription factor ABI5. However, whether and how FyPP3 is regulated at the posttranscriptional level remains unclear. Here, we report that an asparagine-rich protein, NRP, interacts with FyPP3 and tethers FyPP3 to SYP41/61-positive endosomes for subsequent degradation in the vacuole. Upon ABA treatment, the expression of NRP was induced and NRP-mediated FyPP3 turnover was accelerated. Consistently, ABA-induced FyPP3 turnover was abolished in an nrp null mutant. On the other hand, FyPP3 can dephosphorylate NRP in vitro, and overexpression of FyPP3 reduced the half-life of NRP in vivo. Genetic analyses showed that NRP has a positive role in ABA-mediated seed germination and gene expression, and that NRP is epistatic to FyPP3. Taken together, our results identify a new regulatory circuit in the ABA signaling network, which links the intracellular trafficking with ABA signaling.

Imaging cellular distribution of fluorescent supramolecular nanofibers

In this study, we used the 4-nitro-2,1,3-benzoxadiazole(NBD) as an aromatic capping group for a peptide to construct the supramolecular nanofibers. Taking the advantage of the fluorescence property of NBD, we could directly observe the cellular distribution of the self-assembled nanofibers. We found that the distributions of the nanofibers of NBD-FFETIGGY are different in four mammalian cells and two plant cells. The nanofibers are mainly located at the surface of two mammalian cells and one plant cell, while in the intracellular space of other cells. Different distributions of nanofibers lead to different protein binding patterns of the nanofibers in two different cell lines. We believe that a useful and versatile platform has been offered to the image cellular distribution of nanofibers, which can provide useful information to the biological functions of the self-assembled nanostructures.