Tarte Vaishali N, Seok Hye-Yeon, Woo Dong-Hyuk, Le Dinh Huan, Tran Huong T, Baik Ji-Won, Kang In Soon, Lee Sun-Young, Chung Taijoon, Moon Yong-Hwan
Department of Molecular Biology, Pusan National University, Busan, 609-735, Korea.
Plant Cell Rep. 2015 Jul;34(7):1127-38. doi: 10.1007/s00299-015-1771-3. Epub 2015 Feb 18.
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.
拟南芥Qc-SNARE蛋白AtSFT12定位于高尔基体细胞器,通过液泡中Na⁺的积累参与盐胁迫和渗透胁迫反应。为了减轻环境胁迫的有害影响,植物进化出了许多防御机制。在这里,我们使用激活标签法鉴定了一个参与盐胁迫和渗透胁迫反应的拟南芥Qc-SNARE基因AtSFT12。AtSFT12基因的激活标签植株和过表达转基因植株(OXs)都对高浓度的NaCl、LiCl和甘露醇具有耐受性,而功能缺失突变体对NaCl、LiCl和甘露醇敏感。在NaCl、ABA、低温和甘露醇胁迫下AtSFT12转录增加,但在MV处理下不增加。GFP融合的AtSFT12蛋白与高尔基体标记物并列,这意味着其功能与高尔基体介导的运输有关。使用电感耦合等离子体原子发射光谱法对Na⁺进行定量测量,结果显示AtSFT12 OXs积累的Na⁺比野生型植株显著更多。此外,盐处理后,Sodium Green的Na⁺依赖性荧光分析表明,AtSFT12 OX细胞液泡中的Na⁺积累比野生型植物细胞中的更高。综上所述,我们的研究结果表明,高尔基体Qc-SNARE蛋白AtSTF12在盐胁迫和渗透胁迫反应中起重要作用,并通过将Na⁺隔离在液泡中发挥盐胁迫反应功能。