1青枯菌 CysA 蛋白功能的生物信息学研究内容摘要 CysA 蛋白是一种 ABC 转运蛋白，可以将硫酸盐和硫代硫酸盐转运进入细胞。本论文通过对青枯菌 CysA 基因和 CysA 蛋白质进行生物信息方面的分析,蛋白质的结构域、跨膜区域、亲疏性、卷曲螺旋区域、蛋白质的信号肽分别通过 SMART、SOSUl 和 TMHMM、 ProtScale、COILS、SignaIP 等在线网站来预测。最后再预测 CysA 的二级结构和三级结构，同时也预测蛋白质的亚细胞定位，并构建该蛋白的系统发生树。结果分析该蛋白质有一段 AAA 结构域，为亲水性蛋白，无跨膜结构，位于细胞质中，不含卷曲螺旋，也没有信号肽。无规则卷曲与螺旋在 CysA 中占比最大，三级结构呈桶状。从系统发生树上可以看出青枯菌与蒲桃青枯菌、血液病原细菌亲缘关系很近。通过研究发现CysA 蛋白与其它复合体亚基结合共同完成转运硫酸盐和硫代硫酸盐，对青枯菌的生命活动起重要作用，本论文主要分析 CysA 蛋白的功能，为更进一步了解青枯菌提供一些理论依据。【关键词】青枯菌；生物信息；CysA 蛋白 The Research on the Function of CysA Proteins in Ralstonia solanacearum21AbstractCysA is an ABC transporter that transports sulfates and thiosulfates into cells. Here, biological information of bacterial CysA gene and CysA protein was analyzed. The structure of the protein domains, transmembrane region, property, coiled coil area, protein signal peptide respectively by SMART, TMHMM, ProtScale, SOSUI COILS and SignaIP online website to predict. Finally, the secondary structure, tertiary structure and the subcellular localization of the CysA protein were predicted, and the phylogenetic tree of the protein was constructed. The results showed that CysA has a AAA domain. It has no transmembrane structure and is a hydrophilic protein. It doesn't have curly spiral, also have no signal peptide. The a-helix and random coil accounted for the largest proportion in the secondary structure, and the tertiary structure was barrel-shaped. The protein is located in the cytoplasm. Fr...
