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TitleAbilities of the BRICHOS domain to prevent neurotoxicity and fibril formation are dependent on a highly conserved Asp residue.
Journal, issue, pagesRSC Chem Biol, Vol. 3, Issue 11, Page 1342-1358, Year 2022
Publish dateNov 2, 2022
AuthorsGefei Chen / Yuniesky Andrade-Talavera / Xueying Zhong / Sameer Hassan / Henrik Biverstål / Helen Poska / Axel Abelein / Axel Leppert / Nina Kronqvist / Anna Rising / Hans Hebert / Philip J B Koeck / André Fisahn / Jan Johansson /
PubMed AbstractProteins can self-assemble into amyloid fibrils or amorphous aggregates and thereby cause disease. Molecular chaperones can prevent both these types of protein aggregation, but to what extent the ...Proteins can self-assemble into amyloid fibrils or amorphous aggregates and thereby cause disease. Molecular chaperones can prevent both these types of protein aggregation, but to what extent the respective mechanisms are overlapping is not fully understood. The BRICHOS domain constitutes a disease-associated chaperone family, with activities against amyloid neurotoxicity, fibril formation, and amorphous protein aggregation. Here, we show that the activities of BRICHOS against amyloid-induced neurotoxicity and fibril formation, respectively, are oppositely dependent on a conserved aspartate residue, while the ability to suppress amorphous protein aggregation is unchanged by Asp to Asn mutations. The Asp is evolutionarily highly conserved in >3000 analysed BRICHOS domains but is replaced by Asn in some BRICHOS families. The conserved Asp in its ionized state promotes structural flexibility and has a p value between pH 6.0 and 7.0, suggesting that chaperone effects can be differently affected by physiological pH variations.
External linksRSC Chem Biol / PubMed:36349220 / PubMed Central
MethodsEM (single particle)
Resolution17.6 Å
Structure data

EMDB-13005: mutation D148N of recombinant human Bri2 BRICHOS domain,oligomeric state
Method: EM (single particle) / Resolution: 17.6 Å

Source
  • Homo sapiens (human)

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