Schoumacher F, Erny C, Berna A, Godefroy-Colburn T, Stussi-Garaud C
Institut de Biologie Moléculaire des Plantes, Université Louis Pasteur, Strasbourg, France.
Virology. 1992 Jun;188(2):896-9. doi: 10.1016/0042-6822(92)90549-5.
The movement protein of alfalfa mosaic virus (P3) was purified from yeasts transformed with an expression vector containing the P3 gene. Its nucleic acid-binding properties were tested by electrophoretic retardation, nitrocellulose retention, and RNA-protein cross-linking. The recombinant protein had a higher affinity for single-stranded RNA and DNA than for double-stranded nucleic acids. Each nucleic acid molecule bound several protein molecules without sequence specificity. The binding was 80% inhibited by 0.2 M NaCl. These properties are qualitatively similar, but not strictly identical, to those of two other viral movement proteins, the 30-kDa protein of tobacco mosaic virus and the gene I product of cauliflower mosaic virus.
