Abstract
Nuclear proteins isolated from untreated lymphoid cells formed complexes with the interferon-inducible transcriptional enhancer (IITE) containing a 73- and an 84-kDa protein, whereas the nuclear proteins of untreated myeloid cells formed complexes with the IITE which contained 50-, 65-, and 73-, but not 84-kDa nuclear proteins. The difference in the molecular masses of the nuclear proteins binding to the IITE in lymphoid and myeloid cells was due to a phosphatase present in the cytoplasm of the myeloid cells. Induction of transcriptional activation by interferon was accompanied by the binding of a 95-kDa nuclear protein to the IITE 1-4 h after the start of exposure to interferon. Cycloheximide did not inhibit the binding of the 95-kDa nuclear protein or the transcriptional activation of alpha-interferon-inducible genes. These data suggest that the induction of gene transcription by alpha-interferon in hematopoietic cells may be associated with post-translational changes in a 95-kDa nuclear protein that binds to IITE, thereby leading to transcriptional activation.
Highlights
From the Departments of $Hematology and ~Clinicul Immunology Anderson Cancer Center, Houston, Texas 77030 and Biological Therapy, The University of Texas
KDa nuclear protein or the transcriptional activation of a-interferon-inducible genes. These data suggest that the induction of gene transcription by a-interferon in hematopoietic cells may be associated with posttranslational changes in a 95-kDa nuclear protein that binds to inducible transcriptional enhancer (IITE), thereby leading to transcriptional activation
We studied the molecular weights of nuclear proteins isolated from normal and leukemic hematopoietic cells before and after treatment with a-interferon, which bind to interferon-inducible regulatory elements shared by many interferon-inducible genes
Summary
From the Departments of $Hematology and ~Clinicul Immunology Anderson Cancer Center, Houston, Texas 77030 and Biological Therapy, The University of Texas. Induction of transcriptional activation by interferon was accompanied by the binding of a 95-kDa nuclear protein to the IITE l-4 h after the start of exposure to interferon. KDa nuclear protein or the transcriptional activation of a-interferon-inducible genes. These data suggest that the induction of gene transcription by a-interferon in hematopoietic cells may be associated with posttranslational changes in a 95-kDa nuclear protein that binds to IITE, thereby leading to transcriptional activation. The transcriptional activation induced by interferon has been shown to initially involve the posttranslational modification of nuclear proteins which leads to changes in their binding to the interferon-inducible transcriptional enhancer (IITE)’ (2, 6,8)
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