文章基本信息

标题：Trbp111 selectively binds a noncovalently assembled tRNA-like structure
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作者：Tetsuo Kushiro ; Paul Schimmel
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2002
卷号：99
期号：26
页码：16631-16635
DOI：10.1073/pnas.262667999
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Transfer RNAs are key components of the genetic code by virtue of aminoacylation reactions whereby each amino acid is linked to the tRNA that bears the anticodon for the attached amino acid. The L-shaped tRNA structure contains two domains connected at right angles through a corner formed from tertiary interactions involving loops of each domain. Some evidence suggests that the domains arose separately and eventually were fused into a single covalent structure. In this scenario, the present-day tRNA possibly developed through a noncovalently assembled heterodimeric intermediate. Trbp111 is an ancient structure-specific tRNA binding protein that interacts specifically with the outside corner of the L-shaped molecule. Plausibly, this protein could act as a chaperone to cover and protect the fragile corner and thereby have a historical role in the development of tRNA. Here we show that Trbp111 interacts with a noncovalently assembled tRNA-like structure, under conditions where it does not interact with individual tRNA domains. Trbp111 binding specifically requires formation of the tRNA-like corner. In a mixture of RNA domains, it selects those that can make the L-like structure. Thus, cofactors such as Trbp111 have the capacity to help assemble and stabilize RNA dimers that are tRNA-like.