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Sequence specificity of trinucleoside diphosphate binding to polymerized tobacco mosaic virus protein

Nature volume 299, pages 32–36 (1982)Cite this article

Abstract

The binding of trinucleoside diphosphates to long helical rods of tobacco mosaic virus (TMV) protein is shown to depend on base sequence, 5′ AAG 3′ binding being the strongest of the 25 trinucleoside diphosphate sequences measured. As TMV has a stoichiometry of three nucleotides per protein subunit, the sequence of TMV RNA suggested to be the nucleation site for self-assembly of the virus has three possible binding frames. From our binding constant data the most likely frame is predicted and shown to have two contiguous AAG sequences in a hairpin loop region.

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Authors and Affiliations

  1. Biochemistry and Biophysics Section, Biological Sciences Group, University of Connecticut, Storrs, Connecticut, 06268, USA

    John J. Steckert & Todd M. Schuster

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  1. John J. Steckert
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  2. Todd M. Schuster
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Steckert, J., Schuster, T. Sequence specificity of trinucleoside diphosphate binding to polymerized tobacco mosaic virus protein. Nature 299, 32–36 (1982). https://doi.org/10.1038/299032a0

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