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Messenger and aminoacylation functions of brome mosaic virus RNA after chemical modification of 3′ terminus

Nature volume 249, pages 353–355 (1974)Cite this article

Abstract

THE ability of RNA from several plant viruses to bind a specific amino acid in a manner like tRNA is now well established. All members of the tymovirus group so far examined contain RNA which can bind valine1–3; all members of the bromovirus group bind tyrosine (ref. 4 and T.C.H., in preparation), and tobacco mosaic virus (TMV) RNA binds histidine5. The ubiquity of the reaction, and the similarity of the esterification to that of aminoacylation of tRNA indicates that a significant biological function for the property exists. A tRNA-like function such as that of a virus-specific tRNA, or a missense tRNA seems plausible. Although there is evidence that turnip yellow mosaic virus (TYMV) RNA, or a fragment containing the 3′ terminus of TYMV RNA, may donate valine to nascent polypeptides6, it has been established that tyrosine, bound to brome mosaic virus (BMV) RNA, is not donated to peptidyl material in a cell-free system from wheat embryo when directed by viral, plant, or synthetic messenger RNA (ref. 7).

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Authors and Affiliations

  1. Biophysics Laboratory, Graduate School, College of Agricultural and Life Sciences, University of Wisconsin, Madison, Wisconsin, 53706

    D. S. SHIH

  2. Biochemistry Department, College of Agricultural and Life Sciences, University of Wisconsin, Madison, Wisconsin, 53706

    PAUL KAESBERG

  3. Horticulture Department, College of Agricultural and Life Sciences, University of Wisconsin, Madison, Wisconsin, 53706

    T. C. HALL

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  1. D. S. SHIH
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  2. PAUL KAESBERG
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  3. T. C. HALL
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SHIH, D., KAESBERG, P. & HALL, T. Messenger and aminoacylation functions of brome mosaic virus RNA after chemical modification of 3′ terminus. Nature 249, 353–355 (1974). https://doi.org/10.1038/249353a0

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