Journal
PLANT CELL REPORTS
Volume 34, Issue 7, Pages 1127-1138Publisher
SPRINGER
DOI: 10.1007/s00299-015-1771-3
Keywords
Activation tagging; Arabidopsis; AtSFT12; Qc-SNARE; Osmotic stress
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Funding
- National Research Foundation of Korea (NRF) - Ministry of Education, Science and Technology [2012R1A1B3001815, 2014R1A1A2009023]
- Pusan National University
- National Research Foundation of Korea [2012R1A1B3001815, 2014R1A1A2009023] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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AtSFT12, an Arabidopsis Qc-SNARE protein, is localized to Golgi organelles and is involved in salt and osmotic stress responses via accumulation of Na (+) in vacuoles. To reduce the detrimental effects of environmental stresses, plants have evolved many defense mechanisms. Here, we identified an Arabidopsis Qc-SNARE gene, AtSFT12, involved in salt and osmotic stress responses using an activation-tagging method. Both activation-tagged plants and overexpressing transgenic plants (OXs) of the AtSFT12 gene were tolerant to high concentrations of NaCl, LiCl, and mannitol, whereas loss-of-function mutants were sensitive to NaCl, LiCl, and mannitol. AtSFT12 transcription increased under NaCl, ABA, cold, and mannitol stresses but not MV treatment. GFP-fusion AtSFT12 protein was juxtaposed with Golgi marker, implying that its function is associated with Golgi-mediated transport. Quantitative measurement of Na+ using induced coupled plasma atomic emission spectroscopy revealed that AtSFT12 OXs accumulated significantly more Na+ than WT plants. In addition, Na+-dependent fluorescence analysis of Sodium Green showed comparatively higher Na+ accumulation in vacuoles of AtSFT12 OX cells than in those of WT plant cells after salt treatments. Taken together, our findings suggest that AtSTF12, a Golgi Qc-SNARE protein, plays an important role in salt and osmotic stress responses and functions in the salt stress response via sequestration of Na+ in vacuoles.
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