Yang Jin-ying, Sun Ying, Sun Ai-qing, Yi Shu-ying, Qin Jia, Li Ming-hui, Liu Jian
College of Life Science, Shandong Normal University, Jinan, Shandong, 250014, PR China.
Plant Mol Biol. 2006 Oct;62(3):385-95. doi: 10.1007/s11103-006-9027-9. Epub 2006 Aug 16.
The chloroplast HSP100/ClpB is a newly documented member of the ClpB family, but little was known about its role in imparting thermotolerance to cells. A cDNA coding for a HSP100/ClpB homolog has been cloned from Lycopersicon esculentum and termed as Lehsp100/ClpB (the cDNA sequence of Lehsp100/ClpB has been submitted to the GenBank database under accession number: AB219939). The protein encoded by the cDNA was most similar to the putative chloroplast HSP100/ClpBs in higher plants and the ClpB from Cyanobacterium Synechococcus sp. A 97 kDa protein, which matched the predicted size of mature LeHSP100/ClpB, was immunologically detected in chloroplast isolated from heat-treated tomato plants. In addition, the fusion protein, combining the transit sequence of LeHSP100/ClpB and GFP, was found to be located in chloroplast based on the observations of fluorescent microscope images. These results indicated the chloroplast-localization of LeHSP100/ClpB. Both the transcript and the protein of Lehsp100/ClpB were not detected under normal growth conditions, but they were induced by increasingly higher temperatures. An antisense Lehsp100/ClpB cDNA fragment was introduced into the tomato by Agrobacterium-mediated transformation. Antisense lines exhibited an extreme repression of heat-induced expression of Lehsp100/ClpB. The levels of chloroplast HSP60 and small HSP in antisense lines were identical to those of the control plants. After plants preconditioned at 38 degrees C for 2 h were exposed to a lethal heat shock at 46 degrees C for 2 h, the antisense lines were greatly impaired and withered in 21 days of the recovery phase, whereas the untransformed control plants and the vector-transformed plants survived. Furthermore, chlorophyll fluorescence measurements showed that PS II in antisense lines were more susceptible to the thermal irreversible inactivation than the untransformed and vector-transformed control plants. This work provides the first example that induction of chloroplast LeHSP100/ClpB contributes to the acquisition of thermotolerance in higher plants.
叶绿体HSP100/ClpB是ClpB家族新发现的成员,但对其在赋予细胞耐热性方面的作用知之甚少。从番茄中克隆到一个编码HSP100/ClpB同源物的cDNA,命名为Lehsp100/ClpB(Lehsp100/ClpB的cDNA序列已提交至GenBank数据库,登录号为:AB219939)。该cDNA编码的蛋白质与高等植物中假定的叶绿体HSP100/ClpB以及蓝藻集胞藻属的ClpB最为相似。在从热处理番茄植株中分离的叶绿体中,通过免疫检测到一种97 kDa的蛋白质,其大小与预测的成熟LeHSP100/ClpB大小相符。此外,基于荧光显微镜图像观察发现,结合LeHSP100/ClpB转运序列和绿色荧光蛋白(GFP)的融合蛋白定位于叶绿体中。这些结果表明LeHSP100/ClpB定位于叶绿体。在正常生长条件下未检测到Lehsp100/ClpB的转录本和蛋白质,但它们会受到逐渐升高温度的诱导。通过农杆菌介导的转化将反义Lehsp100/ClpB cDNA片段导入番茄。反义株系中Lehsp100/ClpB的热诱导表达受到极度抑制。反义株系中叶绿体HSP60和小HSP的水平与对照植株相同。在38℃预处理2小时的植株经46℃致死热激处理2小时后,反义株系在恢复阶段的21天内严重受损并枯萎,而未转化的对照植株和载体转化植株存活。此外,叶绿素荧光测量表明,反义株系中的PS II比未转化和载体转化的对照植株更容易受到热不可逆失活的影响。这项工作首次证明叶绿体LeHSP100/ClpB的诱导有助于高等植物获得耐热性。