Herpes simplex virus phosphoproteins. II. Characterization of the virion protein kinase and of the polypeptides phosphorylated in the virion.

摘要: The protein kinase associated with purified herpes simplex virus 1 and 2 virions partitioned the capsid-tegument structures was not solubilized by non-ionic detergents low, non-inhibitory concentrations of urea. enzyme required Mg2+ or Mn2+ utilized ATP GTP. activity enhanced Na+ even in presence high Mg2+, but cyclic nucleotides. phosphorylated virion polypeptides only; exogenously added substrates (acidic basic histones, casein, phosphovitin, protamine, bovine serum albumin) were phosphorylated. major species (VP) 1-2, 4, 11-12, 13-14, 18.7, 18.8 23. VP 18.7 have been previously detected, may be forms co-migrating 19. Of remainder, only 23 has identified as a capsid protein; others are constituents tegument under surface envelope. distribution phosphate bound to viral varied depending on concentration pH. In absence dithiothreitol, vitro exchange demonstrable lesser extent two other sequential phosphorylation frist saturating amounts off unlabeled then [gamma-32P]ATP. Analysis specified X recombinants indicates that genes specifying which serve substrate for map unique sequences near left right reinterated DNA L component.