POINT MUTATIONS IN THE HERPES-SIMPLEX VIRUS TYPE-1 VMW110 RING FINGERHELIX AFFECT ACTIVATION OF GENE-EXPRESSION, VIRAL GROWTH, AND INTERACTION WITH PML-CONTAINING NUCLEAR-STRUCTURES

Herpes simplex virus type 1 immediate-early protein Vmw110 (also known as ICP0) has been implicated in the control of the balance between th e lytic and latent states, but the precise mechanisms by which it exer ts its effects are unknown. Vmw110 includes a characteristic zinc bind ing domain, termed the C3HC4 domain or RING finger, which is essential for its function. The solution structure of a related herpes virus RI NG finger domain suggested that an amphipathic alpha helix might be an important functional component of the RING finger. In this paper, we show that the equivalent region of Vmw110 is important for virus growt h in tissue culture and for the normal interaction of Vmw110 with nucl ear structures which include the PML protein.