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The DGCR8 RNA-binding heme domain recognizes primary microRNAs by clamping the hairpin

Jen Quick-Cleveland1, Jose P Jacob1, Sara H Weitz2

  • 1Department of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, CA 90095, USA.

Cell Reports
|June 10, 2014
PubMed

Insights

DGCR8 uses a novel heme-binding domain to recognize microRNA precursors. This interaction is crucial for the Microprocessor complex to process pri-miRNAs effectively.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Canonical primary microRNA transcripts (pri-miRNAs) feature a hairpin structure essential for processing.
  • The Microprocessor complex, comprising Drosha and DGCR8, cleaves pri-miRNAs, but substrate recognition mechanisms are not fully understood.

Purpose of the Study:

  • To elucidate the mechanism by which DGCR8 recognizes pri-miRNA substrates.
  • To investigate the role of DGCR8's heme-binding domain in pri-miRNA recognition and processing.

Main Methods:

  • Biochemical assays to study protein-RNA interactions.
  • Structural analysis of DGCR8-pri-miRNA complexes.
  • Functional assays to assess pri-miRNA processing activity.

Main Results:

  • DGCR8 utilizes a dimeric heme-binding domain, termed RNA-binding heme domain (Rhed), to directly contact pri-miRNAs.
  • Two DGCR8 dimers bind to each pri-miRNA hairpin at opposite ends via their Rheds.
  • The Rhed domain and its heme cofactor are critical for both pri-miRNA binding and processing.
  • Heme is essential for forming processing-competent DGCR8-pri-miRNA complexes.

Conclusions:

  • A novel mode of protein-RNA interaction involving DGCR8's Rhed domain is central to pri-miRNA recognition.
  • A model is proposed where two DGCR8 dimers clamp a pri-miRNA hairpin through their Rheds, facilitating Microprocessor complex function.

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