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Wung, C.H. et al.

Identification of the RNA-binding sites of the triple gene block protein 1 of bamboo mosaic potexvirus.

The triple gene block protein 1 ( TGBp1) encoded by open reading frame 2 of bamboo mosaic potexvirus (BaMV) was overexpressed in Escherichia coli and purified in order to test its RNA-binding activity. UV crosslinking assays revealed that the RNA-binding activity was present mainly in the soluble fraction of the refolded TGBp1. The binding activity was nonspecific and salt concentration-dependent: activity was present at 0-50 mM NaCl but was almost abolished at 200 mM. The RNA-binding domain was located by deletion mutagenesis to the N-terminal 3-24 amino acids of TGBp1. Sequence alignment analysis of the N-terminal 25 amino acids of the TGBp1 homologues of potexviruses identified three arginine residues. Arg-to-Ala substitution at any one of the three arginines eliminated most of the RNA-binding activity, indicating that they were all critical to the RNA-binding activity of the TGBp1 of BaMV.[1]

References

Identification of the RNA-binding sites of the triple gene block protein 1 of bamboo mosaic potexvirus. Wung, C.H., Hsu, Y.H., Liou, D.Y., Huang, W.C., Lin, N.S., Chang, B.Y. J. Gen. Virol. (1999) [Pubmed]

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