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[Interactions between domains within the NH2- and COOH-terminal fragments of presenilins]
1National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, CAMS and PUMC, Beijing 100005, China.
Objective:
To analyze the interactions between domains within the NH2- and COOH-terminal regions of presenilins.
Methods:
The various constructions corresponding to NH2-terminal fragment (NTF) and COOH-terminal fragment (CTF) derivatives of presenilin 1 (PS1) and presenilin 2 (PS2) were generated by RT-PCR, and their interactions were assayed by yeast two-hybrid system.
Results:
Domains within the NH- and COOH-terminal fragments of presenilins could directly interact with each other, and therefore form high molecular weight complex. The interaction site between domains within PS1 located at amino acid 361-447 of PS1 CTF, without the involvement of other partners. Similar interaction was not observed between PS11-360 and PS2341-448, PS2(1)-340 and PS1(361)-467.
Conclusions:
Intramolecular interaction between domains within the NH2- and COOH-terminal regions of presenilins may be critical to the folding and assembly of mature PS molecules.
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