Jung Chang Gyo, Hwang Sun-Goo, Park Yong Chan, Park Hyeon Mi, Kim Dong Sub, Park Duck Hwan, Jang Cheol Seong
Plant Genomics Laboratory, Department of Applied Plant Sciences, Kangwon National University, Chuncheon 200-713, Republic of Korea.
Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute, 1266 Singjeong, Jeongeup 580-185, Jeonbuk, Republic of Korea.
J Plant Physiol. 2015 Mar 15;176:138-46. doi: 10.1016/j.jplph.2015.01.001. Epub 2015 Jan 8.
LRR-RLK (Leucine-Rich Repeat Receptor-Like Kinase) proteins are believed to play essential roles in cell-to-cell communication during various cellular processes including development, hormone perception, and abiotic stress responses. We isolated an LRR-RLK gene previously named Arabidopsis PHLOEM INTERCALATED WITH XYLEM-LIKE 1 (AtPXL1) and examined its expression patterns. AtPXL1 was highly induced by cold and heat stress, but not by drought. The fluorescence signal of 35S::AtPXL1-EGFP was closely localized to the plasma membrane. A yeast two-hybrid and bimolecular fluorescence complementation assay exhibited that AtPXL1 interacts with both proteins, A. thaliana histidine-rich dehydrin1 (AtHIRD1) and A. thaliana light-harvesting protein complex I (AtLHCA1). We found that AtPXL1 possesses autophosphorylation activity and phosphorylates AtHIRD1 and AtLHCA1 in an in vitro assay. Subsequently, we found that the knockout line (atpxl1) showed hypersensitive phenotypes when subjected to cold and heat during the germination stage, while the AtPXL1 overexpressing line as well as wild type plants showed high germination rates compared to the knockout plants. These results provide an insight into the molecular function of AtPXL1 in the regulation of signal transduction pathways under temperature fluctuations.
富含亮氨酸重复序列的类受体激酶(LRR-RLK)蛋白被认为在包括发育、激素感知和非生物胁迫反应在内的各种细胞过程中的细胞间通讯中发挥着重要作用。我们分离出一个先前命名为拟南芥木质部间插韧皮部样1(AtPXL1)的LRR-RLK基因,并检测了其表达模式。AtPXL1在冷胁迫和热胁迫下被高度诱导,但在干旱胁迫下未被诱导。35S::AtPXL1-EGFP的荧光信号紧密定位于质膜。酵母双杂交和双分子荧光互补分析表明,AtPXL1与两种蛋白相互作用,即拟南芥富含组氨酸脱水素1(AtHIRD1)和拟南芥光捕获蛋白复合体I(AtLHCA1)。我们发现AtPXL1具有自磷酸化活性,并在体外实验中使AtHIRD1和AtLHCA1磷酸化。随后,我们发现敲除系(atpxl1)在萌发阶段受到冷胁迫和热胁迫时表现出超敏表型,而与敲除植株相比,AtPXL1过表达系以及野生型植株显示出较高的萌发率。这些结果为深入了解AtPXL1在温度波动下信号转导途径调控中的分子功能提供了线索。