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Purification of the cellular C1 factor required for the stable recognition of the Oct-1 homeodomain by the herpes simplex virus alpha-trans-induction factor (VP16).

The assembly of specific multiprotein complexes on the herpes simplex virus alpha/IE (immediate early) enhancer elements requires the interactions of the Oct-1 POU homeodomain, the viral alpha TIF (alpha-trans-induction factor) (VP16), and at least one additional cellular factor, the C1 factor. The C1 factor interacts directly with alpha TIF, likely forming an intermediate protein complex that recognizes the Oct-1 homeodomain-DNA complex. The biochemical purification of the mammalian C1 factor suggests that it is composed of multiple subunits of related, but heterogeneous, polypeptides. The interaction of a subset of these polypeptides with alpha TIF is stimulated by post-translational modifications of the C1 proteins, suggesting that this factor may be a critical target for the regulation of the herpes simplex virus alpha/IE transcription.

Pubmed ID: 8454622

Authors

  • Kristie TM
  • Sharp PA

Journal

The Journal of biological chemistry

Publication Data

March 25, 1993

Associated Grants

  • Agency: NCI NIH HHS, Id: P01-CA42063
  • Agency: NCI NIH HHS, Id: P30-CA14051

Mesh Terms

  • Amino Acid Sequence
  • Chromatography, High Pressure Liquid
  • DNA-Binding Proteins
  • HeLa Cells
  • Herpes Simplex Virus Protein Vmw65
  • Host Cell Factor C1
  • Humans
  • Macromolecular Substances
  • Molecular Sequence Data
  • Multiprotein Complexes
  • Octamer Transcription Factor-1
  • Phosphorylation
  • Proteins
  • Transcription Factors