first 17 amino acids of the beet necrotic yellow vein virus RNA-5-encoded p26 protein are sufficient to activate transcription in a yeast one-hybrid system

• Published in: Archives of virology Vol. 154; no. 2; pp. 347 - 351
• Main Authors: Covelli, Laura, Klein, Elodie, Gilmer, David
• Format: Journal Article
• Language: English
• Published: Vienna Vienna : Springer Vienna 01-02-2009; Springer Vienna; Springer; Springer Nature B.V
• Subjects: Amino Acid Sequence; Amino acids; Beet necrotic yellow vein virus; Biological and medical sciences; Biomedical and Life Sciences; Biomedicine; Brief Report; Chenopodium quinoa; Chenopodium quinoa - virology; Cloning; E coli; Fundamental and applied biological sciences. Psychology; Gene Expression Regulation, Viral; Infectious Diseases; Localization; Medical Microbiology; Microbiology; Miscellaneous; Molecular Sequence Data; Mutagenesis; Mutation; Phytopathology. Animal pests. Plant and forest protection; Plant Diseases - virology; Plant Viruses - chemistry; Plant Viruses - genetics; Plant viruses and viroids; Plasmids; Protein Structure, Tertiary - genetics; Proteins; RNA Viruses - chemistry; RNA Viruses - genetics; Transcriptional Activation; Two-Hybrid System Techniques; Viral Proteins - genetics; Viral Proteins - metabolism; Virology; Yeast; Beet Necrotic Yellow Vein Virus; SalI Restriction Site; Random Mutagenesis; Aspartic Acid Residue; Transcription Activation Domain; Virus; Yeast; Plant pathogen; Transcription; Benyvirus; Protein; Beet necrotic yellow vein virus
• ISSN: 0304-8608; 1432-8798
• DOI: 10.1007/s00705-008-0306-4

The beet necrotic yellow vein virus (BNYVV) RNA-5-encoded p26 protein is involved in the accentuation of symptoms expression of infected Chenopodium quinoa plants and is capable of transcription activation (TA) in yeast. TA was previously localized within the first 55 residues of the p26 protein. Interestingly, TA did not occur when C-terminally deleted forms of p26 were used. We used a genetic screen in the yeast one-hybrid system to select restored TA from randomly generated mutants. The TA domain was found to be located within the first 17 residues. Alanine replacement of aspartic acids 11, 16, and 17 within the full-length p26 prevented TA but did not impair subcellular localization and the symptom expression.