Isolation of herpes simplex virus regulatory protein ICP4 as a homodimeric complex.

AUTOR(ES)

Metzler, D W

RESUMO

The viral polypeptide ICP4 (or Vmw175) is synthesized during the immediate early phase of infection by herpes simplex virus and regulates the transcription of delayed early and late viral genes. We obtained a partially purified preparation of soluble ICP4 under nondenaturing conditions. Physical constants for native ICP4 were empirically determined by molecular sieve chromatography and sucrose density gradient ultracentrifugation. The Stokes radius of native ICP4 was 8.72 X 10(-7) cm. The sedimentation coefficient of native ICP4 was 9.00S. From these values, the calculated molecular weight of native ICP4 was 342,000, a value which is twice that of monomeric ICP4, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The failure of any other polypeptides to specifically coprecipitate with native ICP4 in the presence of anti-ICP4 antibody indicates that the 342,000-dalton complex is a homodimer of ICP4. The frictional coefficient ratio of native ICP4, which is 1.9, indicates that the homodimer is a highly elongated molecule.

Documentos Relacionados

• Association of herpes simplex virus regulatory protein ICP4 with sequences spanning the ICP4 gene transcription initiation site.
• trans-dominant inhibition of herpes simplex virus transcriptional regulatory protein ICP4 by heterodimer formation.
• Association of the herpes simplex virus regulatory protein ICP4 with specific nucleotide sequences in DNA.
• The herpes simplex virus major regulatory protein ICP4 blocks apoptosis induced by the virus or by hyperthermia.
• Functional interaction and colocalization of the herpes simplex virus 1 major regulatory protein ICP4 with EAP, a nucleolar-ribosomal protein.