Characterization of DNA sequence-common and sequence-specific proteins binding to cis-acting sites for cleavage of the terminal a sequence of the herpes simplex virus 1 genome.

摘要: The terminal 500-base-pair alpha sequence of the herpes simplex virus 1 genome contains signals for cleavage (Pac1 and Pac2) unit-length DNA molecules from concatemers in unique stretches sequences designated Ub Uc, respectively, a cis site DR1. We report that nuclear extracts infected cells contain factors which form two DNA-virus-specific protein complexes with components sequence. Purification forming V2 complex yielded an apparent molecular weight 82,000 binding to non-sequence-specific manner. Addition Mg2+ purified protein-DNA probe mixture resulted exonucleolytic degradation DNA. was identified as virus-specific DNase monoclonal antibody specific viral enzyme. purification proteins V4 weights greater than 250,000 140,000 corresponding cell yet unidentified protein, respectively. These formed sequence-common bands number probes one sequence-specific band containing both Pac2 DR1 but not either alone or Pac1 Since inserted into amplicons induced whereas nonreactive failed induce cleavage, formation this DNA-protein is significant may reflect interaction essential cleavage. possible role study cleavage-packaging capsids presented.