[Interactions between domains within the NH2- and COOH-terminal fragments of presenilins].
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.
Mei
P
P
National Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, CAMS and PUMC, Beijing 100005, China.
Lou
R
R
Li
L
L
Zhou
Y
Y
Gong
J
J
Chen
Y
Y
Wu
G
G
Shen
Y
Y
D001665:Binding Sites; D018076:DNA, Complementary / Q000235:genetics; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D053764:Presenilin-1; D053766:Presenilin-2; D011485:Protein Binding; D020133:Reverse Transcriptase Polymerase Chain Reaction; D020798:Two-Hybrid System Techniques
D018076:DNA, Complementary; D008565:Membrane Proteins; C508853:PSEN1 protein, human; C508861:PSEN2 protein, human; D053764:Presenilin-1; D053766:Presenilin-2