Control of RNA processing by a large non-coding RNA over-expressed in carcinomas

FEBS Lett. 2011 Feb 18;585(4):671-6. doi: 10.1016/j.febslet.2011.01.030. Epub 2011 Jan 23.

Abstract

RNA processing is vital for the high fidelity and diversity of eukaryotic transcriptomes and the encoded proteomes. However, control of RNA processing is not fully established. Σ RNA is a class of conserved large non-coding RNAs (murine Hepcarcin; human MALAT-1) up-regulated in carcinomas. Using antisense technology, we identified that RNA post-transcriptional modification is the most significant global function of Σ RNA. Specifically, processing of the pre-mRNAs of genes including Tissue Factor and Endoglin was altered by hydrolysis of Σ RNA/MALAT-1. These results support the hypothesis that Σ RNA/MALAT-1 is a regulatory molecule exerting roles in RNA post-transcriptional modification.

MeSH terms

  • Alternative Splicing
  • Animals
  • Antigens, CD / genetics
  • Antigens, CD / metabolism
  • Carcinoma / metabolism*
  • Cells, Cultured
  • Endoglin
  • Gene Expression Profiling
  • Gene Expression Regulation, Neoplastic
  • HeLa Cells
  • Humans
  • Nuclear Proteins / metabolism
  • Oligonucleotide Array Sequence Analysis
  • Oligonucleotides, Antisense
  • RNA Precursors / metabolism
  • RNA Processing, Post-Transcriptional*
  • RNA, Long Noncoding
  • RNA, Neoplasm / metabolism*
  • RNA, Untranslated / antagonists & inhibitors
  • RNA, Untranslated / genetics
  • RNA, Untranslated / metabolism*
  • RNA-Binding Proteins / metabolism
  • Rats
  • Receptors, Cell Surface / genetics
  • Receptors, Cell Surface / metabolism
  • Serine-Arginine Splicing Factors
  • Thromboplastin / genetics
  • Thromboplastin / metabolism

Substances

  • Antigens, CD
  • ENG protein, human
  • Endoglin
  • MALAT1 long non-coding RNA, human
  • Malat1 long non-coding RNA, mouse
  • Nuclear Proteins
  • Oligonucleotides, Antisense
  • RNA Precursors
  • RNA, Long Noncoding
  • RNA, Neoplasm
  • RNA, Untranslated
  • RNA-Binding Proteins
  • Receptors, Cell Surface
  • Serine-Arginine Splicing Factors
  • Thromboplastin