Department of Biology, Arizona State University, Tempe, Arizona 85287-1501.
Integr Comp Biol. 2002 Aug;42(4):808-14. doi: 10.1093/icb/42.4.808.
The intertidal zone has historically functioned as an important natural laboratory for testing ideas about how physical factors such as temperature influence organismal physiology and in turn influence the distribution patterns of organisms. Key to our understanding of how the physical environment helps structure organismal distribution is the identification of physiological processes that have ecological relevance. We have focused on biochemical- and molecular-level physiology that would contribute to thermal tolerance and maintenance of a functional intracellular protein pool in the face of extreme and fluctuating environmental temperatures. Past research has addressed processes central to protein homeostasis (e.g., protein ubiquitination) and the molecular ecology of molecular chaperones, a.k.a. heat shock proteins (Hsps), in ectothermic animals. In this presentation, we focus on two new developments regarding the biology of heat shock proteins as molecular chaperones in intertidal organisms. First, we present data on the functional characteristics of the transcriptional factor, HSF1 and discuss how these data relate to the plasticity of Hsp gene expression observed in intertidal organisms in nature. Second, we present data on the biochemical function of heat shock proteins purified from our non-model study organisms and discuss the temperature relationships of these molecules as they assist in protein folding in situ.
潮间带历来是一个重要的自然实验室，可用于检验有关物理因素（如温度）如何影响生物机体生理学，以及反过来如何影响生物分布模式的各种理论。了解物理环境如何帮助构建生物机体分布的关键是确定具有生态相关性的生理过程。我们专注于生物化学和分子水平的生理学，以应对极端和波动的环境温度，从而有助于提高热耐受性和维持细胞内蛋白质库的功能。过去的研究集中于与蛋白质稳态（例如蛋白质泛素化）相关的过程以及分子伴侣（又称热休克蛋白 (Hsp)）的分子生态学，这些研究针对的是变温动物。在本次演讲中，我们重点介绍了有关潮间带生物中热休克蛋白作为分子伴侣的生物学的两个新进展。首先，我们介绍了关于转录因子 HSF1 的功能特征的数据，并讨论了这些数据如何与自然界中观察到的潮间带生物中 HSP 基因表达的可塑性相关。其次，我们介绍了从我们的非模式研究生物中纯化的热休克蛋白的生化功能，并讨论了这些分子在协助原位蛋白质折叠时的温度关系。
