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Gangloff, Y.G., Romier, C., Thuault, S., Werten, S., Davidson, I. (2001). The histone fold is a key structural motif of transcription factor TFIID.  Trends Biochem. Sci. 26(4): 250--257.
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FBrf0156064
Publication Type
Review
Abstract

Transcription factor TFIID is a multiprotein complex composed of the TATA binding protein and its associated factors, and is required for accurate and regulated initiation of transcription by RNA polymerase II. The subunit composition of this factor is highly conserved from yeast to mammals. X-ray crystallography and biochemical experiments have shown that the histone fold motif mediates many of the subunit interactions within this complex. These results, together with electron microscopy and yeast genetics, provide insights into the overall organization of this complex.

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    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Compendium
    Abbreviation
    Trends Biochem. Sci.
    Title
    Trends in Biochemical Sciences
    Publication Year
    1976-
    ISBN/ISSN
    0167-7640 0968-0004
    Data From Reference
    Genes (12)