Circular dichroism of intermediate subviral particles of reovirus. Elucidation of the mechanism underlying the specific monovalent cation effects on uncoating.
1. Circular dichroic (CD) spectra of purified intermediate subviral particles of reovirus were determined in the presence of different monovalent cations. 2. The CD spectra reveal that reo intermediate subviral particles can exist in two conformationally different forms. The two forms are readily distinguished by comparison of their ellipticities in the wavelength regions 210 nm and 220 nm, with a Na+-induced form exhibiting a reduced negative ellipticity relative to a Cs+-induced form. 3. The transition between the Na+- and Cs+-induced forms is reversible by manipulation of the species of monovalent cation present and appears to be temperature independent. 4. Temperature variation studies on dilute suspensions of particles indicate that the Na+-induced form is stable, whereas the Cs+-induced from undergoes a second transition, temperature dependent and irreversible, to become a viral core. 5. A model is presented relating these observations to the known properties of reovirus uncoating and transcriptase activation.
D002586:Cesium; D002942:Circular Dichroism; D012089:Mammalian orthoreovirus 3 / Q000201:enzymology / Q000648:ultrastructure*; D011487:Protein Conformation; D012194:RNA-Directed DNA Polymerase / Q000378:metabolism; D012087:Reoviridae / Q000648:ultrastructure*; D012964:Sodium; D013696:Temperature
D002586:Cesium; D012964:Sodium; D012194:RNA-Directed DNA Polymerase