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Crystallographic characterization of Pap1-DNA complex

Y Fujii1, T Ohira, Y Kyougoku

  • 1Department of Molecular Biology, Nara Institute of Science and Technology (NAIST), 8916-5 Takayama, Ikoma, Nara 630-01, Japan.

Acta Crystallographica. Section D, Biological Crystallography
|October 3, 1998
PubMed
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Pap1, a fission yeast transcription factor, binds non-consensus DNA sequences. Researchers crystallized the Pap1 DNA-binding domain with a non-consensus DNA fragment to understand its function.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Yeast Genetics

Background:

  • Pap1 is a fission yeast transcription factor regulating genes involved in staurosporine resistance, cell growth, cell cycle, carcinogenesis, and differentiation.
  • Pap1 possesses a basic leucine zipper (bZIP) DNA-binding domain but interacts with non-consensus DNA sequences, diverging from typical bZIP binding motifs.

Purpose of the Study:

  • To elucidate the structural basis of Pap1's interaction with non-consensus DNA sequences.
  • To obtain high-resolution structural data of the Pap1 DNA-binding domain complexed with its target DNA.

Main Methods:

  • Crystallization of the Pap1 DNA-binding domain (DBD) complexed with an ATF/CREB-like non-consensus DNA fragment using the vapor-diffusion technique with polyethylene glycol 6000.
  • X-ray diffraction data collection to 2.0 A resolution using a cryo-crystallographic technique.

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Main Results:

  • Highly ordered crystals of the Pap1 DBD-DNA complex were obtained, belonging to space group R3.
  • The crystal structure was determined at 2.0 A resolution, providing detailed insights into the complex's architecture.

Conclusions:

  • The determined structure provides a molecular basis for Pap1's recognition of non-consensus DNA sequences.
  • This structural information is crucial for understanding Pap1's regulatory mechanisms in gene expression and cellular processes.