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TitleStructural evidence that RNA contributes to polymorphism of tau amyloid fibrils.
Journal, issue, pagesiScience, Vol. 29, Issue 4, Page 115501, Year 2026
Publish dateApr 17, 2026
AuthorsRomany Abskharon / Yi Xiao Jiang / Michael R Sawaya / Peng Ge / Jeffrey Zhang / David R Boyer / Joshua L Dolinsky / Justin Pi / Duilio Cascio / Feng Guo / David S Eisenberg /
PubMed AbstractRNA colocalizes with tau deposits in Alzheimer's disease (AD) and drives tau aggregation . Previously, we determined a cryogenic-electron microscopy (cryo-EM) structure of fibrils of full-length tau ...RNA colocalizes with tau deposits in Alzheimer's disease (AD) and drives tau aggregation . Previously, we determined a cryogenic-electron microscopy (cryo-EM) structure of fibrils of full-length tau bound to unfractionated mammalian RNA, revealing a small tau C-terminal core. Here, we present the cryo-EM structure of fibrils of full-length recombinant tau bound to unfractionated mammalian RNA seeded by AD-extracted tau fibrils. This structure reveals an expanded tau C-terminal core resembling AD tau fibrils. RNA sequencing identified 18S ribosomal RNA as the primary fibril-bound species. Next, we determined the cryo-EM structure of fibrils of full-length recombinant tau bound to mammalian 18S ribosomal RNA, revealing a core that consists of the R2 to R4 repeat domains previously seen in pathological tau fibrils. All our recombinant RNA-tau fibrils dissolve upon RNase treatment. Tau fibrils adopt distinct folds in the presence of different RNAs, suggesting RNA is a cofactor capable of shaping tau fibril polymorphism.
External linksiScience / PubMed:42006351 / PubMed Central
MethodsEM (helical sym.)
Resolution3.1 - 3.3 Å
Structure data

70224

9o8e

EMDB-70224, PDB-9o8e:
amyloid fibril of recombinant full-length 2N4R tau complexed with unfractionated mouse liver RNA and seeded by Alzheimer's disease tau fibrils
Method: EM (helical sym.) / Resolution: 3.1 Å

70227

9o8h

EMDB-70227, PDB-9o8h:
amyloid fibril of recombinant full-length 2N4R tau complexed with mouse liver 18S ribosomal RNA
Method: EM (helical sym.) / Resolution: 3.3 Å

Chemicals

ChemComp-CL:
Unknown entry

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / amyloid fibril

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