Purification and Biochemical Characterization of the Promoter-Specific Transcription Factor, Sp1

DOI Web Site 被引用文献17件
  • Michael R. Briggs
    Department of Biochemistry, University of California, Berkeley, CA 94720.
  • James T. Kadonaga
    Department of Biochemistry, University of California, Berkeley, CA 94720.
  • Stephen P. Bell
    Department of Biochemistry, University of California, Berkeley, CA 94720.
  • Robert Tjian
    Department of Biochemistry, University of California, Berkeley, CA 94720.

抄録

<jats:p>The biochemical analysis of cellular trans-activators involved in promoter recognition provides an important step toward understanding the mechanisms of gene expression in animal cells. The promoter selective transcription factor, Sp1, has been purified from human cells to more than 95 percent homogeneity by sequence-specific DNA affinity chromatography. Isolation and renaturation of proteins purified from sodium dodecyl sulfate polyacrylamide gels allowed the identification of two polypeptides (105 and 95 kilodaltons) as those responsible for recognizing and interacting specifically with the GC-box promoter elements characteristic of Sp1 binding sites.</jats:p>

収録刊行物

  • Science

    Science 234 (4772), 47-52, 1986-10-03

    American Association for the Advancement of Science (AAAS)

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