ERH facilitates microRNA maturation through the interaction with the N-terminus of DGCR8

Nucleic Acids Res. 2020 Nov 4;48(19):11097-11112. doi: 10.1093/nar/gkaa827.

Abstract

The microprocessor complex cleaves the primary transcript of microRNA (pri-miRNA) to initiate miRNA maturation. Microprocessor is known to consist of RNase III DROSHA and dsRNA-binding DGCR8. Here, we identify Enhancer of Rudimentary Homolog (ERH) as a new component of Microprocessor. Through a crystal structure and biochemical experiments, we reveal that ERH uses its hydrophobic groove to bind to a conserved region in the N-terminus of DGCR8, in a 2:2 stoichiometry. Knock-down of ERH or deletion of the DGCR8 N-terminus results in a reduced processing of suboptimal pri-miRNAs in polycistronic miRNA clusters. ERH increases the processing of suboptimal pri-miR-451 in a manner dependent on its neighboring pri-miR-144. Thus, the ERH dimer may mediate 'cluster assistance' in which Microprocessor is loaded onto a poor substrate with help from a high-affinity substrate in the same cluster. Our study reveals a role of ERH in the miRNA biogenesis pathway.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Cycle Proteins / metabolism*
  • HCT116 Cells
  • HEK293 Cells
  • Humans
  • K562 Cells
  • MicroRNAs / metabolism
  • Protein Binding
  • Protein Conformation
  • RNA Processing, Post-Transcriptional*
  • RNA-Binding Proteins / metabolism*
  • Transcription Factors / metabolism*

Substances

  • Cell Cycle Proteins
  • DGCR8 protein, human
  • ERH protein, human
  • MIRN144 microRNA, human
  • MIRN451 microRNA, human
  • MicroRNAs
  • RNA-Binding Proteins
  • Transcription Factors