タバコモザイクウイルスの形態形成における核酸の認識機構

概要

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Coat proteins of tobacco mosaic virus (TMV) recognize the sequence of AAG on RNA at the initiation of assembly and then bind to any nucleotides during elongation. To understand the molecular mechanism of such specific and non-specific interactions, we studied the elementary interaction patterns by using model crystals which contain amino-acid side chains and nucleic-acid bases. It was found that the carboxyl group tends to form a double hydrogen bond to all kinds of bases at the sites where Watson-Crick type pairing usually occurs. This common structural feature is effective to non-specific binding, because there is no need to move largely for polypeptide chain. Hydrogen bond energies calculated by molecular orbital methods indicate the strongest interaction with guanine in the order of G > C ≅ A > U ≅ T. These data, together with other elementary interactions, are then applied successfully to construct a binding model of the coat proteins with RNA. Reassembly experiments of TMV using di- and tri-nucleotides supported the model.
日本結晶学会の論文