FSML- Improvements to El Verde Station, Puerto Rico

温度胁迫对植物造成了独特的和不断升级的问题，因为它们是环境的固定俘虏。植物和其他生物一样，通过特异性表达热激蛋白来响应温度升高。这些蛋白质是植物对包括高温在内的许多胁迫产生耐受性反应所必需的。 然而，这些蛋白在胁迫耐受中的具体功能在很大程度上是未知的。 初步的实验已经证明了一个特定的和突出的热休克蛋白，热休克蛋白17.7，在耐热性的作用，通过使用反义技术，以减少这种蛋白质的表达。 拟议的实验将调查为什么表达Hspl7.7 mRNA的反义版本的植物是不耐热的，并应提供深入了解植物耐热性的整体过程。 反义Hsp17.7植物显示Hsp17.7以及其他非相关Hsps水平的显著降低。 发生这种情况的潜在分子机制将通过使用基因特异性探针和特异性抗体定量分析mRNA和蛋白质水平来解决。 分析将集中在转基因和对照细胞的转录，翻译和蛋白质加工和营业额的过程。此外，Hsp17.7的潜在伴侣功能将使用标准测定法进行评估。

Temperature stress poses a unique and escalating problem to plants since they are immobile captives of the environment. Plants, like all other organisms, respond to increasing temperature by the specific expression of heat shock proteins. These proteins are essential for the plant to mount a tolerance response to many stresses including higher temperatures. However the specific functions of these proteins in stress tolerance is largely unknown. Preliminary experiments have demonstrated a role for one specific and prominent heat shock protein, Hsp17.7, in thermotolerance, by using antisense technology to decrease the expression of this protein. The proposed experiments will investigate why the plants expressing an antisense version of Hspl7.7 mRNA are less thermotolerant and should provide insight into the overall process of plant thermotolerance. Antisense Hspl7.7 plants show dramatic decreases in the levels of Hspl7.7 as well as other non-related Hsps. The underlying molecular mechanisms by which this occurs will be addressed by quantitative analysis of mRNA and protein levels using gene specific probes and specific antibodies. The analysis will focus on the processes of transcription, translation and protein processing and turnover in transgenic and control cells. In addition, the potential chaperone function of Hsp17.7 will be assessed using standard assays.