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Related Experiment Videos

Searching for DNA-protein interactions by lambda phage display.

Carla Cicchini1, Helenia Ansuini, Laura Amicone

  • 1Dipartimento di Biotecnologie Cellulari ed Ematologia, Sezione di Genetica Molecolare, Fondazione Istituto Pasteur-Cenci Bolognetti, Università La Sapienza, 00161, Rome, Italy.

Journal of Molecular Biology
|September 25, 2002
PubMed
Summary

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Phage display identified specific DNA-binding domains interacting with gene regulatory elements. This powerful method aids in discovering proteins that bind to DNA regulatory sequences.

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Understanding DNA-protein interactions is crucial for gene regulation.
  • Phage display is a versatile technique for identifying molecular interactions.

Purpose of the Study:

  • To apply phage display technology for identifying DNA-binding domains.
  • To investigate interactions with the HNF1alpha gene promoter sequence.

Main Methods:

  • Generated a cDNA expression library on bacteriophage lambda from murine hepatic cells.
  • Selected the library using the HNF1alpha promoter sequence.
  • Confirmed binding using phage-independent assays, ELISA, and South-Western blotting.

Main Results:

Related Experiment Videos

  • Identified specific DNA-binding domains interacting with the HNF1alpha promoter.
  • One domain matched known DNA-binding proteins.
  • Discovered multiple adjacent DNA-binding sites with a common motif.

    • Conclusions:

    • Phage display is an effective strategy for identifying DNA-binding proteins.
    • This method facilitates the discovery of proteins interacting with DNA regulatory elements.