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A rapid affinity method for isolation and characterization of sequence specific DNA binding factor.

R P Singh, V Natarajan

    Biochemical and Biophysical Research Communications
    |August 31, 1987
    PubMed
    Summary
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    Researchers purified a specific transcription factor crucial for adenovirus IVa2 promoter activity using avidin-biotin affinity chromatography. This method achieved a 12,000-fold purification, aiding in understanding gene regulation.

    Area of Science:

    • Molecular Biology
    • Biochemistry
    • Virology

    Background:

    • Transcription factors are essential regulators of gene expression.
    • Understanding adenovirus IVa2 promoter regulation requires identifying its specific transcription factors.

    Purpose of the Study:

    • To isolate and purify the sequence-specific DNA binding factor for the adenovirus IVa2 promoter.
    • To characterize the purification of this transcription factor using affinity chromatography.

    Main Methods:

    • Developed an affinity chromatography technique utilizing avidin monomer and biotin interaction.
    • Biotinylated a 432 bp adenovirus IVa2 promoter fragment (152-160 bp upstream of start site).
    • Purified the transcription factor from HeLa cell extract using an avidin monomer column and NaCl gradients.

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    Main Results:

    • Successfully isolated a sequence-specific DNA binding factor.
    • Achieved a 12,000-fold purification of the adenovirus IVa2 transcription factor.
    • Confirmed factor purification through band retardation assays.

    Conclusions:

    • Avidin-biotin affinity chromatography is an effective method for purifying transcription factors.
    • The purified factor specifically binds to the upstream region of the adenovirus IVa2 promoter.
    • This purification facilitates further studies on adenovirus gene regulation.