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Inhibition of chaperonin GroEL by a monomer of ovine prion protein and its oligomeric forms

Authors
  • Kudryavtseva, S. S.1
  • Stroylova, Y. Y.1
  • Zanyatkin, I. A.2
  • Haertle, T.3
  • Muronetz, V. I.1, 2
  • 1 Lomonosov Moscow State University, Belozersky Institute of Physico-Chemical Biology, Moscow, 119234, Russia , Moscow (Russia)
  • 2 Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow, 119234, Russia , Moscow (Russia)
  • 3 Institut National de la Recherche Agronomique, Nantes, 44000, France , Nantes (France)
Type
Published Article
Journal
Biochemistry (Moscow)
Publisher
Pleiades Publishing
Publication Date
Oct 19, 2016
Volume
81
Issue
10
Pages
1213–1220
Identifiers
DOI: 10.1134/S0006297916100199
Source
Springer Nature
Keywords
License
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Abstract

The possibility of inhibition of chaperonin functional activity by amyloid proteins was studied. It was found that the ovine prion protein PrP as well as its oligomeric and fibrillar forms are capable of binding with the chaperonin GroEL. Besides, GroEL was shown to promote amyloid aggregation of the monomeric and oligomeric PrP as well as PrP fibrils. The monomeric PrP was shown to inhibit the GroEL-assisted reactivation of the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH). The oligomers of PrP decelerate the GroEL-assisted reactivation of GAPDH, and PrP fibrils did not affect this process. The chaperonin GroEL is capable of interacting with GAPDH and different PrP forms simultaneously. A possible role of the inhibition of chaperonins by amyloid proteins in the misfolding of the enzymes involved in cell metabolism and in progression of neurodegenerative diseases of amyloid nature is discussed.

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