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作 者:李岱容[1] 穆柳青[2] 张春燕[2] 杨春[2]
机构地区:[1]重庆医科大学附属第一医院呼吸科,重庆400016 [2]重庆医科大学病原微生物教研室,重庆400016
出 处:《遵义医学院学报》2014年第1期57-61,共5页Journal of Zunyi Medical University
基 金:国家自然科学基金资助项目(NO:81101216)
摘 要:目的对结核分枝杆菌的基因clpC2(Rv2667)的同源基因进行序列分析和相似性比较,并对其编码蛋白进行理化性质及功能的预测,为ClpC2蛋白的结构与功能研究提供基础技术资料。方法根据GeneBank中分枝杆菌clpC2同源基因的核苷酸序列,进行多重序列比对和进化树构建;应用ExPA Sy在线序列分析工具,对结核分枝杆菌ClpC2蛋白质理化性质及保守结构域进行预测;应用Gene ontology(GO)在线软件对ClpC2蛋白酶的功能进行分析。结果 clpC2系统进化树分析,与16 s rRNA基因相比,进化距离明显变大,而在结核分枝杆菌复合群中高度保守。ClpC2蛋白为亲水性非跨膜蛋白,在细胞质表达,具有水解和催化功能,是一个依赖于ATP的Clp亚单位。结论 clpC2基因在结核分枝杆菌复合群中高度保守,其编码的蛋白ClpC2是一个依赖于ATP的水解蛋白酶。Objective To provide evidence for further research on the structures and functions of Rv2667 gene encoding ClpC2 protein in Mycobacterium tuberculosis, this study analyzed and predicted the physical and chemi- cal characteristics of Mycobacterium tuberculosis ClpC2, and compared its nucleotide sequence similarity among myeobacteria. Methods According to the NCBI clpC2 gene sequence of Mycobacterium tuberculosis, multiple se- quence alignment and phylogenetic - tree - construction were performed. Physicochemical properties and con- served domain of ClpC2 protein in Mycobacterium tuberculosis was predicted with ExPASy online tools; The func- tion of ClpC2 protease was analyzed by Gene Ontology (GO) online software. Results Compared with the 16s rRNA gene, evolutionary distance is significantly bigger. ClpC2 protein is hydrophilic, a non -transmembrane protein, expressed in endoplasmic reticulum, with hydrolysis and catalytic function, and an ATP -independent Clp subunit. Conclusion ClpC2 is conservative highly in Mycobacterium tuberculosis complex, and its encoding protein is an ATP- independent proteolytic enzyme.
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