Abstract
The products of in vitro reconstitution of brome mosaic virus (BMV) protein and RNA were studied using analytical sedimentation and polyacrylamide gel electrophoresis. The product formed depended on the protein concentration, even though the ratio of RNA to protein was constant (1:4). At a low ionic strength with protein at 0.2 g/liter, mostly 78 S particles (like native BMV) were made, whereas at 2 g/liter of protein, reconstitution proceeded erratically. When the ionic strength was decreased to various levels by dialysis after mixing RNA and protein at I = 1.0, the four RNAs were encapsidated at different rates according to species, with RNAs 4 and 3 at the highest rates. The same sequential encapsidation in order of increasing molecular weight occurred as the ratio of protein to RNA was increased. Some particles containing three copies of the smallest RNA were found. These observations show that BMV protein displays in vitro a differential affinity for the various BMV RNA species.
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