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Related Experiment Videos

TRF1 is a dimer and bends telomeric DNA

A Bianchi1, S Smith, L Chong

  • 1The Rockefeller University, New York, NY 10021, USA.

The EMBO Journal
|April 1, 1997
PubMed
Summary
This summary is machine-generated.

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Telomere protein TRF1 binds DNA as a dimer, requiring two Myb repeats for stable complex formation. This dimerization and DNA bending mechanism is similar to yeast Rap1p, suggesting conserved telomere functions.

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • TRF1 is a mammalian protein that binds to telomeric DNA sequences (TTAGGG repeats).
  • TRF1 shares homology with Myb transcription factors but possesses only one Myb-type DNA-binding motif.

Purpose of the Study:

  • To investigate the DNA-binding mechanism of TRF1.
  • To compare TRF1's function with yeast telomeric protein Rap1p.

Main Methods:

  • Yeast two-hybrid assay to study protein-protein interactions.
  • DNA-binding assays to analyze complex formation and DNA bending.

Main Results:

  • TRF1 forms dimers through a conserved N-terminal domain, both in complex with DNA and in yeast two-hybrid assays.

Related Experiment Videos

  • TRF1 dimers require both Myb repeats for stable DNA binding, similar to other Myb-related proteins.
  • TRF1 bends telomeric DNA by approximately -120 degrees, a property shared with yeast Rap1p.

    • Conclusions:

    • TRF1 functions as a dimer, utilizing its Myb repeats for DNA binding.
    • The DNA-binding and DNA-bending properties of TRF1 suggest conserved mechanisms for telomere function in yeast and mammals.