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Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex.

The RNA-binding protein Y14 binds preferentially to mRNAs produced by splicing and is a component of a multiprotein complex that assembles approximately 20 nucleotides upstream of exon-exon junctions. This complex probably has important functions in post-splicing events including nuclear export and nonsense-mediated decay of mRNA. We show that Y14 binds to two previously reported components, Aly/REF and RNPS1, and to the mRNA export factor TAP. Moreover, we identified magoh, a human homolog of the Drosophila mago nashi gene product, as a novel component of the complex. Magoh binds avidly and directly to Y14 and TAP, but not to other known components of the complex, and is found in Y14-containing mRNPs in vivo. Importantly, magoh also binds to mRNAs produced by splicing upstream (approximately 20 nucleotides) of exon- exon junctions and its binding to mRNA persists after export. These experiments thus reveal specific protein-protein interactions among the proteins of the splicing-dependent mRNP complex and suggest an important role for the highly evolutionarily conserved magoh protein in this complex.

Pubmed ID: 11707413

Authors

  • Kataoka N
  • Diem MD
  • Kim VN
  • Yong J
  • Dreyfuss G

Journal

The EMBO journal

Publication Data

November 15, 2001

Associated Grants

None

Mesh Terms

  • Animals
  • Cell Fractionation
  • Cell Line
  • Cell Nucleus
  • Cytoplasm
  • DNA, Complementary
  • Drosophila
  • Drosophila Proteins
  • Evolution, Molecular
  • Exons
  • Glutathione Transferase
  • HeLa Cells
  • Humans
  • Microscopy, Fluorescence
  • Models, Biological
  • Nuclear Proteins
  • Oocytes
  • Plasmids
  • Precipitin Tests
  • Protein Binding
  • Protein Structure, Tertiary
  • RNA Splicing
  • RNA, Messenger
  • Recombinant Fusion Proteins
  • Ribonuclease H
  • Two-Hybrid System Techniques
  • Xenopus