Chimeric CA2+/Calmodulin-Dependent Protein Kinase in Plants

植物中的嵌合 CA2/钙调蛋白依赖性蛋白激酶

• 批准号: 9630337
• 负责人: B. Poovaiah
• 金额: --
• 依托单位: Washington State University
• 依托单位国家: 美国
• 项目类别: Continuing grant
• 财政年份: 1996
• 资助国家: 美国
• 起止时间: 1996-09-15 至 1999-08-31
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=9630337&HistoricalAwards=false
• 关键词: Chimeric; CA2+; Calmodulin; Dependent; Protein

Abstract 9630337 Poovaiah Protein phosphorylation is one of the major mechanisms for transducing extracellular signals to intracellular responses. Calcium is important in mediating a number of signaling pathways, and Ca+/Calmodulin (CM) regulated protein phosphorylation amplifies and modifies Ca mediated signals. Several Ca/CaM dependent protein kinases have been well characterized in mammalian systems, but little is known about Ca/CaM dependent protein kinases in plants. The laboratory of the PI has cloned a chimeric Ca/CaM dependent protein kinase gene from developing anthers. This CCaMk contains a catalytic domain, a CaM binding domain and a visin-like Ca binding domain in one polypeptide. This protein is distinct form other known plant and animal kinases, and its structure suggests it may have evolved from the fusion of two genes that are functionally and phylogenetically diverse. This is the first evidence for a Ca/CaM dependent protein kinase in plants. In this grant the structure function relationships of CCaMK as well as the effects of altered levels in the plant, will be examined. Deletion and point mutants will be studied to determine the function of the regulatory domain, and the role of autophosphorylation sites will be confirmed using site directed mutants. Synthetic peptides will be used to identify and study the autoinhibitory domain. The effect of altered expression of CCaMK will be observed in transgenic plants with sense or antisense constructs of the CCaMK gene. These studies should establish the presence and the role of this important enzyme in plants. *** ***

摘要9630337 Poovaiah蛋白的磷酸化是将细胞外信号转导为细胞内反应的主要机制之一。钙在许多信号转导通路中起重要作用，钙/钙调蛋白(CM)调节的蛋白质磷酸化放大和修饰了钙介导的信号。一些依赖于钙/钙调素的蛋白激酶在哺乳动物系统中已经得到了很好的描述，但对植物中的依赖于钙/钙调素的蛋白激酶却知之甚少。PI的实验室已经从发育中的花药中克隆了一个嵌合的钙/钙调素依赖性蛋白激酶基因。该CCaMk在一个多肽中含有一个催化结构域、一个CaM结合域和一个类似Visin的钙结合域。该蛋白与其他已知的动植物蛋白激酶不同，它的结构表明它可能是由两个功能和系统发育不同的基因融合而来的。这是植物中存在钙/钙调素依赖性蛋白激酶的第一个证据。在这项授权中，将研究CCaMK的结构功能关系以及植物中水平变化的影响。将研究缺失和点突变以确定调节域的功能，并将使用定点突变来确认自动磷酸化位点的作用。人工合成的多肽将被用来识别和研究自抑制结构域。CCaMK基因表达改变的影响将在CCaMK基因的正义或反义构建的转基因植物中观察到。这些研究应该确定这种重要酶在植物中的存在和作用。*