{'fraction_non_alphanumeric': 0.04019138755980861, 'fraction_numerical': 0.03827751196172249, 'mean_word_length': 5.046242774566474, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
[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.