Biogenesis of mammalian microRNAs by a non-canonical processing pathway

Nucleic Acids Res. 2012 May;40(10):4626-40. doi: 10.1093/nar/gks026. Epub 2012 Jan 23.

Abstract

Canonical microRNA biogenesis requires the Microprocessor components, Drosha and DGCR8, to generate precursor-miRNA, and Dicer to form mature miRNA. The Microprocessor is not required for processing of some miRNAs, including mirtrons, in which spliceosome-excised introns are direct Dicer substrates. In this study, we examine the processing of putative human mirtrons and demonstrate that although some are splicing-dependent, as expected, the predicted mirtrons, miR-1225 and miR-1228, are produced in the absence of splicing. Remarkably, knockout cell lines and knockdown experiments demonstrated that biogenesis of these splicing-independent mirtron-like miRNAs, termed 'simtrons', does not require the canonical miRNA biogenesis components, DGCR8, Dicer, Exportin-5 or Argonaute 2. However, simtron biogenesis was reduced by expression of a dominant negative form of Drosha. Simtrons are bound by Drosha and processed in vitro in a Drosha-dependent manner. Both simtrons and mirtrons function in silencing of target transcripts and are found in the RISC complex as demonstrated by their interaction with Argonaute proteins. These findings reveal a non-canonical miRNA biogenesis pathway that can produce functional regulatory RNAs.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Argonaute Proteins / metabolism
  • Argonaute Proteins / physiology
  • Cell Line
  • Cells, Cultured
  • Gene Silencing
  • Humans
  • Introns
  • Mice
  • MicroRNAs / metabolism*
  • Proteins / physiology
  • RNA Processing, Post-Transcriptional*
  • RNA-Binding Proteins
  • Ribonuclease III / metabolism
  • Ribonuclease III / physiology

Substances

  • Ago2 protein, mouse
  • Argonaute Proteins
  • DGCR8 protein, human
  • MIRN1225 microRNA, human
  • MicroRNAs
  • Proteins
  • RNA-Binding Proteins
  • DROSHA protein, human
  • Ribonuclease III