ABSTRACT
Figure 1. Presenilin sequence alignment. Amino acid sequences of presenilins from mammals (represented by human PS1 and PS2), Xenopus laevis (X-PS-α and X-PS-β), C. elegans (SEL-12 and SPE-4), and Drosophila melanogaster (DPS) are aligned, with abbreviated names indicated to the left. Amino acids that are conserved in at least four proteins are drawn in white on black background. Yellow boxes indicate predicted transmembrane (TM) domains (as suggested by Hardy, 1997a). The residues mutated in FAD linked and C.elegans presenilins are indicated, together with the
S182) and Iq42.1 (Takano et al., 1997) (PS2: initially labeled STM2) and encode proteins of 467 and 448 amino acids, respectively, which are 67% identical in primary sequence. They are highly similar
replacing residue. Red: PS1 mutations and ∆exon10 deletion, blue: PS2 mutations, green: sel-12 mutations; magenta: spe-4 deletion. The data for these figures are mostly taken from de Silva and Patel (1997) and from Hardy (1997a,b). (See Colour Plate II)
to the presenilins of rat and mouse. The 468 amino acid rat presenilin-1 protein has 88% and 93% amino acid similarity with those of human PS1 and mouse PS1, respectively (Takahashi et al., 1996).
