MAPPING OF THE RNA-BINDING DOMAIN OF THE ALFALFA MOSAIC-VIRUS MOVEMENT PROTEIN

In-frame contiguous deletions were created in the movement protein gen e of alfalfa mosaic virus by site-directed mutagenesis. The mutated mo vement proteins were expressed in Escherichia coil, extracted and then purified by denaturing gel electrophoresis and then renatured. Their binding ability with RNA was assayed by electrophoretic retardation an d u.v.-crosslinking. Results indicated that a domain included within a mino acids 36 to 81 was necessary for RNA binding.