Genomic organization of the mouse fertilin β gene that encodes an ADAM family protein active in sperm-egg fusion
- 1 January 1997
- journal article
- research article
- Published by Wiley in Developmental Genetics
- Vol. 20 (4) , 320-328
- https://doi.org/10.1002/(sici)1520-6408(1997)20:4<320::aid-dvg3>3.0.co;2-9
Abstract
The fertilin α and β genes (Ftna and Ftnb, respectively) encode a sperm surface heterodimer that functions in sperm–egg fusion. They are the first identified members of a large gene family coding for multidomain membrane proteins (ADAMs) that include A Disintegrin And Metalloprotease domain. In this study, we report the isolation and structural organization of the mouse fertilin β gene. The gene is present as a single copy and covers a region of approximately 55 kilobases in the genome. The fertilin β gene is composed of at least 20 exons interrupted by 19 introns. The sizes of the exons are relatively small and vary from 56 to 193 bases; the sizes of introns vary from 350 bases to 9.4 kilobases. The exon–intron boundaries conform to the GT/AG rule with one exception: GC replaces GT at the 5′ splice site in intron 13. Comparison of genomic organization between mouse fertilin β and the previously sequenced ADAM family gene, human MDC [Katagiri et al. (1995): Cytogenet Cell Genet 68:39–44] showed 12 conserved exon–intron boundaries. In addition, we analyzed the fertilin α gene, demonstrating that more than one gene is present in the mouse genome. Dev. Genet. 20:320–328, 1997.Keywords
This publication has 29 references indexed in Scilit:
- Molecular Cloning of the Human Fertilin β SubunitBiochemical and Biophysical Research Communications, 1996
- Chromosomal Assignment of Four Testis-Expressed Mouse Genes from a New Family of Transmembrane Proteins (ADAMs) Involved in Cell–Cell Adhesion and FusionGenomics, 1996
- The Molecules of Mammalian FertilizationCell, 1996
- ADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions.The Journal of cell biology, 1995
- A metalloprotease-disintegrin participating in myoblast fusionNature, 1995
- Human metalloprotease/disintegrin-like (MDC) gene: exon-intron organization and alternative splicingCytogenetic and Genome Research, 1995
- Multiple roles for PH-20 and fertilin in sperm-egg interactionsSeminars in Developmental Biology, 1994
- Evidence that proteolysis of the surface is an initial step in the mechanism of formation of sperm cell surface domains.The Journal of cell biology, 1990
- 5′ cleavage site in eukaryotic pre-mRNA splicing is determined by the overall 5′ splice region, not by the conserved 5′ GUCell, 1987
- Identification and purification of a sperm surface protein with a potential role in sperm-egg membrane fusion.The Journal of cell biology, 1987