HSP70-related 65 kDa protein of beet yellows closterovirus is a microtubule-binding protein

• Published in: FEBS letters 1992-06, Vol.304 (1), p.12-14
• Main Authors: Karasev, Alexander V., Kashina, Anna S., Gelfand, Vladimir I., Dolja, Valerian V.
• Format: Article
• Language: English
• Subjects: 70 kDa heat-shock proteins; 90 kDa heat-shock proteins; Animals; beet yellows virus; BYV; Cattle; Cell-to-cell movement; Cloning, Molecular; Electrophoresis, Polyacrylamide Gel; Heat-Shock Proteins - genetics; Heat-Shock Proteins - metabolism; HSP70; HSP90; microtubule; Microtubule-associated protein; Microtubule-Associated Proteins - genetics; Microtubule-Associated Proteins - metabolism; open reading frame; ORF; Plant virus; Plant Viruses - genetics; Plant Viruses - metabolism; potato virus X; Protein Binding; PVX; Sequence Homology, Nucleic Acid; Viral Proteins - genetics; Viral Proteins - metabolism
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(92)80578-5

Beet yellows virus (BYV) genome encodes a 65 kDa protein homologous to the HSP70 family of cellular heat-shock proteins (Agranovsky, A.A., Boyko, V.P., Karasev, A.V., Koonin, E.V. and Dolja, V.V. (1991) J. Mol. Biol. 217, 603–610). The respective gene was cloned and expressed in vitro yielding a product of the expected size (p65). This product was found to bind to the purified microtubules with a binding constant of 4 × 10 −7 M. The binding of p65 was stimulated if ATP presented in the translation mixture was hydrolyzed by apyrase. Removal of the short C-terminal domains of α- and β-tubulin by subtilisin digestion abolished the binding, demonstrating its specificity. The possible role of p65 association with microtubules in the movement of virus within and/or between plant cells is proposed.