Characterization of presenilin-amyloid precursor interaction using bacterial expression and two-hybrid systems for human membrane proteins.
Characterization of presenilin-amyloid precursor interaction using bacterial expression and two-hybrid systems for human membrane proteins.
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使用细菌表达和人膜蛋白双杂交系统表征早老素-淀粉样蛋白前体相互作用。
DOI：
10.1080/09687860400008429
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发表时间：
2004
影响因子：
--
通讯作者：
Ehrmann,Michael
中科院分区：
文献类型：
--
作者：
Harnasch,Mona;Grau,Sandra;Behrends,Christian;Dove,SimonL;Hochschild,Ann;Iskandar,Maria-Karnina;Xia,Weiming;Ehrmann,Michael
用大肠杆菌生产人膜蛋白早老素1和淀粉样前体蛋白，并分析它们之间的相互作用。我们的数据表明，淀粉样前体蛋白的主要结合位点位于早老素的N-末端三个跨膜段，而不是在建议的活性位点含有两个保守的天冬氨酸残基。这些数据还表明在PS1的C-末端存在足够疏水性的额外片段，以潜在地充当跨膜片段。这些发现的γ-分泌酶的功能的影响进行了讨论。
AnEscherichia colisystem 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.