A Short Basic Domain Supports a Nucleic Acid-Binding Activity in the Rice Tungro Bacilliform Virus Open Reading Frame 2 Product
| Autor: | Mario Keller, Emmanuel Jacquot, Pierre Yot |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
Recombinant Fusion Proteins
Lysine chemistry.chemical_compound Open Reading Frames Viral Proteins Virology Amino Acid Sequence Badnavirus Rice tungro bacilliform virus chemistry.chemical_classification Genetics biology RNA RNA-Binding Proteins Oryza biology.organism_classification Amino acid Protein Structure Tertiary DNA-Binding Proteins Open reading frame Biochemistry chemistry DNA Viral Nucleic acid RNA Viral Cacao swollen-shoot virus DNA |
| Zdroj: | Virology. 239(2):352-359 |
| ISSN: | 0042-6822 |
| DOI: | 10.1006/viro.1997.8859 |
| Popis: | Little is known about the features of badnavirus open reading frame 2 products (P2). So far, no consensus functional domain has been found in these proteins. However, they all have in common at their C-terminus amino acids which may have the capacity to bind nucleic acids. Such capacity has already been established for cacao swollen shoot virus protein P2. We have looked for such a binding capacity of rice tungro bacilliform virus (RTBV) ORF 2 product. For this purpose, the protein was expressed as full-length or truncated versions inEscherichia coli.When used in nucleic acid-binding assays, complete RTBV P2 was shown to bind both DNA and RNA. This property may be related to a basic sequence, PPKKGIKRKYPA, localized at its C-terminus. Mutations were introduced into this sequence and revealed that four of the five basic residues, including a crucial lysine, are required for the binding to nucleic acids. Moreover, this sequence can confer binding capacity when it is fused to the N-terminus of nonbinding proteins. |
| Databáze: | OpenAIRE |
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