期刊
SCIENCE
卷 367, 期 6483, 页码 1230-+出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aba3526
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资金
- UK Medical Research Council [MC_UP_A025_1013]
- Stowers Institute for Medical Research
- MRC [MC_UP_A025_1013] Funding Source: UKRI
How long-lived memories withstand molecular turnover is a fundamental question. Aggregates of a prion-like RNA-binding protein, cytoplasmic polyadenylation element-binding (CPEB) protein, is a putative substrate of long-lasting memories. We isolated aggregated Drosophila CPEB, Orb2, from adult heads and determined its activity and atomic structure, at 2.6-angstrom resolution, using cryo-electron microscopy. Orb2 formed similar to 75-nanometer-long threefold-symmetric amyloid filaments. Filament formation transformed Orb2 from a translation repressor to an activator and seed for further translationally active aggregation. The 31-amino acid protofilament core adopted a cross-beta unit with a single hydrophilic hairpin stabilized through interdigitated glutamine packing. Unlike the hydrophobic core of pathogenic amyloids, the hydrophilic core of Orb2 filaments suggests how some neuronal amyloids could be a stable yet regulatable substrate of memory.
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