3'-Terminal 2'-O-methylation of lung cancer miR-21-5p enhances its stability and association with Argonaute 2

Nucleic Acids Res. 2020 Jul 27;48(13):7027-7040. doi: 10.1093/nar/gkaa504.

Abstract

Methylation of miRNAs at the 2'-hydroxyl group on the ribose at 3'-end (2'-O-methylation, 2'Ome) is critical for miRNA function in plants and Drosophila. Whether this methylation phenomenon exists for mammalian miRNA remains unknown. Through LC-MS/MS analysis, we discover that majority of miR-21-5p isolated from human non-small cell lung cancer (NSCLC) tissue possesses 3'-terminal 2'Ome. Predominant 3'-terminal 2'Ome of miR-21-5p in cancer tissue is confirmed by qRT-PCR and northern blot after oxidation/β-elimination procedure. Cancerous and the paired non-cancerous lung tissue miRNAs display different pattern of 3'-terminal 2'Ome. We further identify HENMT1 as the methyltransferase responsible for 3'-terminal 2'Ome of mammalian miRNAs. Compared to non-methylated miR-21-5p, methylated miR-21-5p is more resistant to digestion by 3'→5' exoribonuclease polyribonucleotide nucleotidyltransferase 1 (PNPT1) and has higher affinity to Argonaute-2, which may contribute to its higher stability and stronger inhibition on programmed cell death protein 4 (PDCD4) translation, respectively. Our findings reveal HENMT1-mediated 3'-terminal 2'Ome of mammalian miRNAs and highlight its role in enhancing miRNA's stability and function.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Apoptosis Regulatory Proteins / metabolism
  • Argonaute Proteins / metabolism*
  • Carcinoma, Non-Small-Cell Lung / metabolism*
  • Exoribonucleases / metabolism
  • Gene Expression Regulation, Neoplastic
  • Humans
  • Lung Neoplasms / metabolism*
  • Methylation
  • Methyltransferases / metabolism*
  • MicroRNAs / metabolism*
  • RNA-Binding Proteins / metabolism

Substances

  • AGO2 protein, human
  • Apoptosis Regulatory Proteins
  • Argonaute Proteins
  • MIRN21 microRNA, human
  • MicroRNAs
  • PDCD4 protein, human
  • RNA-Binding Proteins
  • Methyltransferases
  • HENMT1 protein, human
  • Exoribonucleases
  • PNPT1 protein, human