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首页> 外文期刊>Journal of Molecular Biology >MODIFICATION OF PRIMARY STRUCTURES OF HAIRPIN RIBOZYMES FOR PROBING ACTIVE CONFORMATIONS
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MODIFICATION OF PRIMARY STRUCTURES OF HAIRPIN RIBOZYMES FOR PROBING ACTIVE CONFORMATIONS

机译：修饰发夹状核酶主要结构以探究活性构象

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摘要

Hairpin ribozymes consist of two stem-loop domains, and these domains are assumed to interact with each other to produce the self-cleavage activity We have studied the relationship of the tertiary structure of the hairpin ribozyme and the cleavage activity by dividing and re-joining the domains. A hairpin ribozyme (E50) was divided at the hinge region, and the main part was joined to a substrate (S1) using tri-or penta-cytidylates. These ribozymes retained the cleavage activity in the presence of the rest of the molecule, indicating that the active conformation could be maintained if the two domains interacted with each other. Based on the these results, we designed a new type of hairpin ribozyme by replacing one of the domains. To maintain the interaction of the domains, oligocytidylates were inserted at a junction. These reversely joined ribozyme complexes showed cleavage activity that was dependent on the linker lengths. These modifications in the primary structure of the hairpin ribozyme confirm the structural requirement for the catalytic reaction and provide information for the correlation of the tertiary structure with the cleavage of the hairpin ribozyme. (C) 1995 Academic Press Limited [References: 29]
机译：发夹状核酶由两个茎-环结构域组成，并且假定这些结构域彼此相互作用以产生自切割活性。域。发夹状核酶（E50）在铰链区分开，并且主要部分使用三或五cytydylates连接到基板（S1）。这些核酶在分子其余部分的存在下保留了切割活性，表明如果两个结构域彼此相互作用，则可以保持活性构象。根据这些结果，我们通过替换一个域来设计一种新型的发夹状核酶。为了维持结构域的相互作用，在连接处插入寡聚胞苷。这些反向连接的核酶复合物显示裂解活性，其取决于接头的长度。发夹状核酶一级结构的这些修饰证实了催化反应的结构要求，并为三级结构与发夹状核酶裂解的相关性提供了信息。 （C）1995 Academic Press Limited [参考：29]

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