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Related Experiment Videos

DNA recognition by beta-sheets in the Arc repressor-operator crystal structure

B E Raumann1, M A Rould, C O Pabo

  • 1Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.

Nature
|February 24, 1994
PubMed
Summary
This summary is machine-generated.

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The Arc repressor tetramer-operator complex structure reveals how bacteriophage P22 regulates gene transcription. This study details unique DNA binding and dimer interactions critical for lytic growth.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Virology

Background:

  • Bacteriophage P22 lytic growth involves gene transcription regulated by the Arc repressor.
  • The Arc repressor binds cooperatively as a tetramer to a specific operator DNA sequence.

Purpose of the Study:

  • To determine the co-crystal structure of the Arc repressor tetramer-operator complex.
  • To elucidate the molecular mechanisms of transcriptional regulation by Arc repressor.

Main Methods:

  • Co-crystal X-ray diffraction at 2.6 A resolution.
  • Structural analysis of protein-DNA interactions.

Main Results:

  • The Arc tetramer binds to a 21-base-pair operator site.
  • Each Arc dimer recognizes DNA via an antiparallel beta-sheet in the major groove.

Related Experiment Videos

  • Arc-DNA interactions are less symmetrical than homologous repressors, with conformational changes in the beta-sheet upon binding.
  • Dimer-dimer interactions involve a distinct protein surface compared to MetJ repressor.

    • Conclusions:

    • The determined structure provides detailed insights into the Arc repressor's DNA binding mechanism.
    • Structural differences highlight unique regulatory strategies in bacteriophage P22.
    • This work advances understanding of repressor-operator complex formation and transcriptional control.