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TitleCryo-EM structure of a neuronal functional amyloid implicated in memory persistence in .
Journal, issue, pagesScience, Vol. 367, Issue 6483, Page 1230-1234, Year 2020
Publish dateMar 13, 2020
AuthorsRuben Hervas / Michael J Rau / Younshim Park / Wenjuan Zhang / Alexey G Murzin / James A J Fitzpatrick / Sjors H W Scheres / Kausik Si /
PubMed AbstractHow 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 ...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 CPEB, Orb2, from adult heads and determined its activity and atomic structure, at 2.6-angstrom resolution, using cryo-electron microscopy. Orb2 formed ~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-β 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.
External linksScience / PubMed:32165583 / PubMed Central
MethodsEM (helical sym.)
Resolution2.6 Å
Structure data

21316

6vps

EMDB-21316, PDB-6vps:
Cryo-EM structure of the amyloid core of Drosophila Orb2 isolated from head
Method: EM (helical sym.) / Resolution: 2.6 Å

Source
  • drosophila melanogaster (fruit fly)
KeywordsPROTEIN FIBRIL / amyloid / prion-like / long-term memory

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