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Crystal structure of human DGCR8 core

Sun Young Sohn1, Won Jin Bae, Jeong Joo Kim

  • 1National Creative Research Center for Structural Biology and Department of Life Science, Pohang University of Science and Technology, Hyo-ja dong, San31, Pohang, KyungBook 790-784, South Korea.

Nature Structural & Molecular Biology
|August 21, 2007
PubMed

Insights

The DGCR8 protein, crucial for microRNA maturation, binds pri-miRNA substrates. Its structure reveals how DGCR8 recognizes these substrates, enabling microRNA processing.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • The Drosha-DGCR8 complex initiates microRNA (miRNA) maturation by cleaving primary miRNA (pri-miRNA).
  • Drosha possesses the catalytic activity, while DGCR8 (or Pasha) anchors the pri-miRNA substrate.
  • Understanding DGCR8's substrate recognition mechanism is key to elucidating miRNA biogenesis.

Purpose of the Study:

  • To determine the crystal structure of the human DGCR8 core (DGCR8S).
  • To elucidate the molecular basis of pri-miRNA recognition by DGCR8.
  • To propose a model for DGCR8-pri-miRNA interaction.

Main Methods:

  • X-ray crystallography to determine the structure of human DGCR8 core (residues 493-720).
  • Fluorescent resonance energy transfer (FRET) analysis.
  • Site-directed mutagenesis studies.

Main Results:

  • The crystal structure revealed a pseudo two-fold symmetry in the arrangement of DGCR8's two double-stranded RNA-binding domains (dsRBDs).
  • The H2 helix within each dsRBD was identified as critical for pri-miRNA substrate recognition.
  • Structural and biochemical data suggest DGCR8 recognizes pri-miRNA in two distinct orientations.

Conclusions:

  • The determined structure provides insights into the molecular architecture of the DGCR8 core.
  • DGCR8 employs its dsRBDs, particularly the H2 helix, for pri-miRNA binding.
  • A model for DGCR8-mediated pri-miRNA recognition is proposed, advancing understanding of miRNA processing.

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