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首页> 外文期刊>Journal of Molecular Biology >Specific tyrosylation of the bulky tRNA-like structure of brome mosaic virus RNA relies solely on identity nucleotides present in its amino acid-accepting domain.
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Specific tyrosylation of the bulky tRNA-like structure of brome mosaic virus RNA relies solely on identity nucleotides present in its amino acid-accepting domain.

机译：溴化花叶病毒RNA的庞大tRNA样结构的特定酪氨酰化仅依赖于其氨基酸接受域中存在的同一性核苷酸。

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摘要

Residues specifying aminoacylation by yeast tyrosyl-tRNA synthetase (TyrRS) of the tRNA-like structure present at the 3'-end of brome mosaic virus (BMV) RNA were determined by the in vitro approach using phage T7 transcripts. They correspond to nucleotides equivalent to base-pair C1-G72 and discriminator base A73 in the amino acid-acceptor branch of the molecule. No functional equivalents of the tyrosine anticodon residues, shown to be weakly involved in tyrosine identity of canonical tRNA(Tyr), were found in the BMV tRNA-like structure. This indicates a behaviour of this large and intricate molecule reminiscent of that of a minihelix derived from an amino acid-acceptor branch. Furthermore, iodine footprinting experiments performed on a tyrosylable BMV RNA transcript of 196 nt complexed to yeast TyrRS indicate that the amino acid-acceptor branch of the viral RNA is protected against cleavages as well as a hairpin domain, which is possibly located perpendicularly to its accepting branch. This domain without the canonical anticodon loop or the tyrosine anticodon acts as an anchor for TyrRS interaction leading to a better efficiency of tyrosylation. Copyright 2001 Academic Press.
机译：通过使用噬菌体T7转录本的体外方法，确定了通过酵母酪氨酰-tRNA合成酶（TyrRS）对存在于布鲁姆花叶病毒（BMV）RNA 3'末端的tRNA样结构进行氨基酰化的残基。它们对应于与分子的氨基酸受体分支中的碱基对C1-G72和鉴别基A73等同的核苷酸。在BMV tRNA样结构中未发现酪氨酸反密码子残基的功能等同物，该功能同弱地参与了典型tRNA（Tyr）的酪氨酸识别。这表明这种大而复杂的分子的行为使人联想到衍生自氨基酸受体分支的小螺旋。此外，对与酵母TyrRS复合的196 nt的可酪氨酰BMV RNA转录本进行的碘足迹实验表明，病毒RNA的氨基酸受体分支受到保护，可防止切割以及发夹结构域，该结构可能与其受体垂直科。没有规范的反密码子环或酪氨酸反密码子的此域充当TyrRS相互作用的锚点，从而导致更好的酪氨酰化效率。版权所有2001学术出版社。

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