MAGOH interacts with a novel RNA-binding protein

MAGOH is the human homologue of Drosophila mago nashi, a protein that is re quired for normal germ plasm development in the Drosophila embryo, Using hu man 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 c ontaining a conserved RNA-binding region. This gene, designated RBM8, encod es 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 betwee n MAGOH and RBM8 was demonstrated by both yeast two-hybrid and GST fusion p rotein pull-down assays. Like MAGOH, RBM8 gene is expressed ubiquitously in human tissues; three species of RBM8 mRNA were detected. Also similar to M AGOH, RBM8 expression is serum inducible in quiescent NIH3T3 fibroblast cel ls. (C) 2000 Academic Press.