MAGOH interacts with a novel RNA-binding protein

Genomics. 2000 Jan 1;63(1):145-8. doi: 10.1006/geno.1999.6064.

Abstract

MAGOH is the human homologue of Drosophila mago nashi, a protein that is required for normal germ plasm development in the Drosophila embryo. Using human MAGOH as a bait protein in a yeast two-hybrid screen, we recovered four independent cDNA clones that encode different lengths of a novel protein containing a conserved RNA-binding region. This gene, designated RBM8, encodes a 173-aa protein that was shown to have an apparent molecular mass of 26 kDa, as demonstrated by in vitro translation assay. The interaction between MAGOH and RBM8 was demonstrated by both yeast two-hybrid and GST fusion protein pull-down assays. Like MAGOH, RBM8 gene is expressed ubiquitously in human tissues; three species of RBM8 mRNA were detected. Also similar to MAGOH, RBM8 expression is serum inducible in quiescent NIH3T3 fibroblast cells.

Publication types

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

MeSH terms

  • 3T3 Cells
  • Amino Acid Sequence
  • Animals
  • Blood Proteins / genetics
  • Blood Proteins / metabolism
  • Brain / metabolism
  • Cloning, Molecular
  • DNA, Complementary / genetics
  • Humans
  • Mice
  • Molecular Sequence Data
  • Nuclear Proteins / metabolism*
  • RNA, Messenger / analysis
  • RNA-Binding Proteins / genetics*
  • RNA-Binding Proteins / metabolism
  • Sequence Alignment
  • Two-Hybrid System Techniques
  • Yeasts

Substances

  • Blood Proteins
  • DNA, Complementary
  • MAGOH protein, human
  • Magoh protein, mouse
  • Nuclear Proteins
  • RBM8A protein, human
  • RNA, Messenger
  • RNA-Binding Proteins

Associated data

  • GENBANK/AF198620