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a Department of Biology, Tufts University, Medford, Massachusetts 02155
b Center for Molecular Medicine and Genetics, Wayne State University School of Medicine, Detroit, Michigan 48202
c The Jackson Laboratory, Bar Harbor, Maine 04609
Here we report the isolation and characterization of mouse testicular cDNAs encoding the mammalian homologue of the Xenopus germ cell-specific nucleic acid-binding protein FRGY2 (mRNP3+4), hereafter designated MSY2. MSY2 is a member of the Y box multigene family of proteins; it contains the cold shock domain that is highly conserved among all Y box proteins and four basic/aromatic islands that are closely related to the other known germline Y box proteins from Xenopus, FRGY2, and goldfish, GFYP2. Msy2 undergoes alternative splicing to yield alternate N-terminal regions upstream of the cold shock domain. Although MSY2 is a member of a large family of nucleic acid-binding proteins, Southern blotting detects only a limited number of genomic DNA fragments, suggesting that Msy2 is a single copy gene. By Northern blotting and immunoblotting, MSY2 appears to be a germ cell-specific protein in the testis. Analysis of Msy2 mRNA expression in prepubertal and adult mouse testes, and in isolated populations of germ cells, reveals maximal expression in postmeiotic round spermatids, a cell type with abundant amounts of stored messenger ribonucleoproteins. In the ovary, MSY2 is present exclusively in diplotene-stage and mature oocytes. MSY2 is maternally inherited in the one-cell-stage embryo but is not detected in the late two-cell-stage embryo. This loss of MSY2 is coincident with the bulk degradation of maternal mRNAs in the two-cell embryo.
2 Correspondence: Norman B. Hecht, Center for Research on Reproduction and Women's Health and Department of Obstetrics and Gynecology, University of Pennsylvania Medical Center, 752 Clinical Research Building/6142, Philadelphia, PA 19104–6142, FAX: 215 573 5408; or Mary T. Murray, Center for Molecular Medicine and Genetics, Wayne State University School of Medicine, Detroit, MI 48202.
3 Present address: Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, New York 10461
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