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  • 1
    Publication Date: 1992-09-04
    Description: Cloning of the mammalian basic transcription factors serves as a major step in understanding the mechanism of transcription initiation. The 62-kilodalton component (p62) of one of these transcription factors, BTF2 was cloned and overexpressed. A monoclonal antibody to this polypeptide inhibited transcription in vitro. Immunoaffinity experiments demonstrated that the 62-kilodalton component is closely associated with the other polypeptides present in the BTF2 factor. Sequence similarity suggests that BTF2 may be the human counterpart of RNA polymerase II initiation factor b from yeast.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fischer, L -- Gerard, M -- Chalut, C -- Lutz, Y -- Humbert, S -- Kanno, M -- Chambon, P -- Egly, J M -- New York, N.Y. -- Science. 1992 Sep 4;257(5075):1392-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de Genetique Moleculaire des Eucaryotes, Centre National de la Recherche Scientifique, Unite 184, Faculte de Medecine, Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1529339" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Cloning, Molecular ; Escherichia coli/genetics ; Gene Expression ; HeLa Cells ; Humans ; Immunoblotting ; Molecular Sequence Data ; Molecular Weight ; Oligonucleotide Probes ; Recombinant Proteins/chemistry ; Sequence Homology, Nucleic Acid ; Transcription Factor TFIIH ; Transcription Factors/chemistry/*genetics ; *Transcription Factors, TFII ; Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 1993-04-02
    Description: The human BTF2 basic transcription factor (also called TFIIH), which is similar to the delta factor in rat and factor b in yeast, is required for class II gene transcription. A strand displacement assay was used to show that highly purified preparation of BTF2 had an adenosine triphosphate-dependent DNA helicase activity, in addition to the previously characterized carboxyl-terminal domain kinase activity. Amino acid sequence analysis of the tryptic digest generated from the 89-kilodalton subunit of BTF2 indicated that this polypeptide corresponded to the ERCC-3 gene product, a presumed helicase implicated in the human DNA excision repair disorders xeroderma pigmentosum and Cockayne's syndrome. These findings suggest that transcription and nucleotide excision repair may share common factors and hence may be considered to be functionally related.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schaeffer, L -- Roy, R -- Humbert, S -- Moncollin, V -- Vermeulen, W -- Hoeijmakers, J H -- Chambon, P -- Egly, J M -- New York, N.Y. -- Science. 1993 Apr 2;260(5104):58-63.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉UPR 6520 (CNRS), Unite 184 (INSERM), Faculte de Medecine, Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8465201" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/pharmacology ; Binding Sites ; Cockayne Syndrome/enzymology/genetics ; DNA/metabolism ; DNA Helicases/metabolism ; *DNA Repair ; Humans ; Immunoblotting ; Peptide Fragments ; Promoter Regions, Genetic ; Protein Kinases/metabolism ; RNA Polymerase II/metabolism ; Recombinant Proteins/metabolism ; Sequence Analysis ; Transcription Factor TFIIH ; Transcription Factors/*metabolism ; *Transcription Factors, TFII ; Transcription, Genetic ; Trypsin/metabolism ; Xeroderma Pigmentosum/enzymology/genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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