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Abstract
An Escherichia coli system was used to produce the human membrane proteins presenilin 1 and amyloid precursor protein and to analyse their interaction. Our data indicate that the main binding site for amyloid precursor protein is located in the N-terminal three-transmembrane segments of presenilin and not in the proposed active site containing the two conserved aspartate residues. The data also suggest the presence of an additional segment of sufficient hydrophobicity at the C-terminus of PS1 to act potentially as a transmembrane segment. The implications of these findings for the function of γ-secretase are discussed.
PS1, presenilin; APP, amyloid precursor protein; C99, fragment of APP containing the C-terminal 99 residues; Aβ, amyloid β-protein; TM, transmembrane segment; cI, Lambda repressor, LacZ, β-galactosidase; PAA, protein-A agarose; DDM, dodecylmaltoside; PhoA, alkaline phosphatase; ω, omega sub-unit of RNA polymerise
PS1, presenilin; APP, amyloid precursor protein; C99, fragment of APP containing the C-terminal 99 residues; Aβ, amyloid β-protein; TM, transmembrane segment; cI, Lambda repressor, LacZ, β-galactosidase; PAA, protein-A agarose; DDM, dodecylmaltoside; PhoA, alkaline phosphatase; ω, omega sub-unit of RNA polymerise