1887

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Volume 80, Issue 5

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

Abstract

The triple gene block protein 1 (TGBp1) encoded by open reading frame 2 of bamboo mosaic potexvirus (BaMV) was overexpressed in 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 m NaCl but was almost abolished at 200 m. 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.

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© Journal of General Virology 1999
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1999-05-01
2024-04-19
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Identification of the RNA-binding sites of the triple gene block protein 1 of bamboo mosaic potexvirus
J. Gen. Virol. 80, 1119 (1999); https://doi.org/10.1099/0022-1317-80-5-1119
/content/journal/jgv/10.1099/0022-1317-80-5-1119
/content/journal/jgv/10.1099/0022-1317-80-5-1119
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