SWI2/SNF2 ATPase CHR2 remodels pri-miRNAs via Serrate to impede miRNA production

Nature. 2018 May;557(7706):516-521. doi: 10.1038/s41586-018-0135-x. Epub 2018 May 16.

Abstract

Chromatin remodelling factors (CHRs) typically function to alter chromatin structure. CHRs also reside in ribonucleoprotein complexes, but little is known about their RNA-related functions. Here we show that CHR2 (also known as BRM), the ATPase subunit of the large switch/sucrose non-fermentable (SWI/SNF) complex, is a partner of the Microprocessor component Serrate (SE). CHR2 promotes the transcription of primary microRNA precursors (pri-miRNAs) while repressing miRNA accumulation in vivo. Direct interaction with SE is required for post-transcriptional inhibition of miRNA accumulation by CHR2 but not for its transcriptional activity. CHR2 can directly bind to and unwind pri-miRNAs and inhibit their processing, and this inhibition requires the remodelling and helicase activity of CHR2 in vitro and in vivo. Furthermore, the secondary structures of pri-miRNAs differed between wild-type Arabidopsis thaliana and chr2 mutants. We conclude that CHR2 accesses pri-miRNAs through SE and remodels their secondary structures, preventing downstream processing by DCL1 and HYL1. Our study uncovers pri-miRNAs as a substrate of CHR2, and an additional regulatory layer upstream of Microprocessor activity to control miRNA accumulation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Adenosine Triphosphatases / metabolism*
  • Arabidopsis / enzymology*
  • Arabidopsis / genetics
  • Arabidopsis Proteins / metabolism*
  • Gene Expression Regulation, Plant
  • MicroRNAs / biosynthesis*
  • MicroRNAs / genetics
  • MicroRNAs / metabolism
  • Protein Binding
  • RNA Folding
  • RNA Processing, Post-Transcriptional
  • RNA-Binding Proteins / metabolism*
  • Transcription, Genetic

Substances

  • Arabidopsis Proteins
  • MicroRNAs
  • RNA-Binding Proteins
  • SE protein, Arabidopsis
  • Adenosine Triphosphatases
  • BRM protein, Arabidopsis