Gibson C W, Golub E E, Abrams W R, Shen G, Ding W, Rosenbloom J
Department of Anatomy, University of Pennsylvania School of Dental Medicine, Philadelphia 19104.
Biochemistry. 1992 Sep 8;31(35):8384-8. doi: 10.1021/bi00150a036.
The amelogenins are the most abundant proteins in developing tooth enamel. Previous analyses have demonstrated that transcriptionally active genes encoding the proteins are located on both the bovine X and the bovine Y chromosomes. We report here the cloning and sequence analysis of the Y-chromosomal gene and corresponding cDNA. The Y-specific mRNA encodes a translation product in which a 21 amino acid domain has been deleted, relative to the X-specific amelogenin, resulting in loss of a structure tentatively described as a beta-spiral. There are also 13 single amino acid differences compared to the X-specific amelogenin. In addition, we have cloned and sequenced an X-chromosomal alternatively spliced amelogenin cDNA that encodes a 43 amino acid amelogenin primary translation product. Hydrophobicity analysis indicates that all analyzed amelogenin proteins have a mean hydrophilic character and the two peptides translated from alternatively spliced messages have significant increases in percentage of hydrophobic amino acids.