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Related Experiment Videos

Determinants of sequence-specific DNA-binding by p48v-myb.

A Garcia1, K LaMontagne, D Reavis

  • 1Department of Microbiology, School of Medicine, State University of New York, Stony Brook 11794-8621.

Oncogene
|February 1, 1991
PubMed
Summary

The avian myeloblastosis virus myb oncogene protein (p48v-myb) binds DNA specifically. Its amino-terminal domain is crucial for this sequence-specific DNA-binding, interacting with flanking nucleotides.

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Area of Science:

  • Molecular Biology
  • Oncogenesis
  • Virology

Background:

  • The v-myb oncogene, derived from avian myeloblastosis virus, encodes a nuclear protein (p48v-myb).
  • This protein is known to bind DNA in a sequence-specific manner, playing a role in oncogenesis.

Purpose of the Study:

  • To investigate the protein and DNA determinants governing the sequence-specific DNA-binding of p48v-myb.
  • To identify the minimal protein domain required for DNA binding and characterize the DNA recognition site.

Main Methods:

  • Expression of wild-type and mutant p48v-myb proteins in E. coli.
  • Analysis of DNA-binding activity using sequence-specific binding assays.
  • Site-directed mutagenesis to probe protein domains involved in DNA binding.

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Main Results:

  • The highly conserved amino-terminal domain of p48v-myb is essential for sequence-specific DNA-binding.
  • Neither of the tandem 50 amino acid repeats within this domain is sufficient on its own for binding.
  • p48v-myb recognizes a single consensus myb binding site and binds DNA as a monomer.
  • Sequence-specific binding necessitates nucleotides flanking the previously identified PyAACT/GG consensus sequence.

Conclusions:

  • The amino-terminal domain contains the core DNA-binding function of p48v-myb.
  • The precise DNA sequence, including flanking nucleotides, is critical for high-affinity binding.
  • Understanding these determinants provides insight into the mechanism of v-myb oncogene function.