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Validation of Amelogenesis Imperfecta Inferred from Amelogenin Evolution

¹ UMR 7138, Equipe "Evolution & Développement du Squelette", Université Paris 6, Case 05, 7 quai St-Bernard, 75005 Paris, France; and
² Department of Histology, The Nippon Dental University, School of Dentistry, Niigata, Japan

View larger version (18K): [in this window] [in a new window]   Figure 1. Relationships of the amniote lineages (in bold) for which amelogenin was used in this study (adapted from Madsen et al., 2001; Murphy et al., 2001; Janke et al., 2005; Vidal and Hedges, 2005). The number of species in each clade is indicated between the brackets. See APPENDIX 1 for information on the species and sequences.

View larger version (34K): [in this window] [in a new window]   Figure 2. Amino-acid sequence of human amelogenin with indication of important residues inferred from the alignment of 52 mammalian sequences (A) and of 80 amniote sequences (52 mammals, 6 crocodiles, and 22 squamates) (B). (The alignments are presented in APPENDIX 2.) Exon 4 (14 residues) was not included, because it was absent in most species studied. Signal peptide is on the grey background. The protein sequence (191 amino acids) is numbered from methionine (1). Large characters = residues unchanged; italics = residues that can be substituted for by an amino acid from the same group only. Small characters = residues for which substitution can be made. Boldface characters = the 5 residues known to lead to amelogenesis imperfecta after substitution.