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作 者:杨卓茹 张敏敏 蔡汝洁 张含笑 管俊豪 Altaf Ahmed Simair 陆昌瑞 YANG Zhuo-ru;ZHANG Min-min;CAI Ru-jie;ZHANG Han-xiao;GUAN Jun-hao;Ahaf Ahmed Simair;LU Chang-rui(College of Chemistry,Chemical Engineering and Bioteehnology,Donghua University,Shanghai 201620,China)
机构地区:[1]东华大学化学化工与生物工程学院,上海201620
出 处:《生物学杂志》2018年第4期97-99,共3页Journal of Biology
基 金:国家自然科学基金(31300603);中央高校基本科研基金(15D110508;15D110527;13D110522;17D210502;17D310512;2232014D3-39);国家大学生创新实验项目(14T10501);上海高校特聘教授(东方学者)计划(No.2012-28);东华大学创新实验计划项目(X171051707);东华大学化学化工与生物工程学院创新实验计划项目(17T10518);中国博士后科研基金特别资助(2015M571455)
摘 要:端粒酶是一类独特的核糖核蛋白复合物,能够维持真核生物染色体末端端粒的完整性。目前,人端粒酶全酶分子组装机制及其结构与功能的关系知之甚少,人端粒酶RNA(human telomerase RNA,hTR)的结构研究也仅限于二级结构。通过对hTR CR4/5结构域进行体外转录、纯化,利用X射线小角散射技术(small-angle x-ray scattering,SAXS),获得其在溶液中的聚集信息,并预测分析了hTR CR4/5的构象。这将对hTR CR4/5结构域及hTR三维结构的解析提供有利的数据支持,为了解hTR在端粒酶逆转录过程中的功能提供实验数据。Telomerase is a specialized reverse transcriptase which is responsible for maintaining integrity of telomere at the end of eukaryotic chromosomes. The current study about molecular assembly mechanism of human telomerase holoenzyme and its relationship between structure and function are seldom involved. The structural research of human telomerase RNA (hTR) is so far limited to its secondary structure. In this study, hTR CR4/5 domain was produced by in vitro transcription and purification, and its assembly information as well as conformation in solution was analyzed using small angle X-ray scattering (SAXS) technology. The results could be valuable information for research of hTR CR4/5 domain and hTR three-dimensional structure, and promote cognition of the function that hTR in the process of telomerase reverse transcriptase.
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