| Autor: |
Winter R; Institute for Biochemistry and Biotechnology, Technical Biochemistry, Martin-Luther-University Halle-Wittenberg, 06120 Halle (Saale), Germany., Kühn U, Hause G, Schwarz E |
| Jazyk: |
angličtina |
| Zdroj: |
The Journal of biological chemistry [J Biol Chem] 2012 Jun 29; Vol. 287 (27), pp. 22662-71. Date of Electronic Publication: 2012 May 08. |
| DOI: |
10.1074/jbc.M112.362327 |
| Abstrakt: |
Oculopharyngeal muscular dystrophy is a late-onset disease caused by an elongation of a natural 10-alanine segment within the N-terminal domain of the nuclear poly(A)-binding protein 1 (PABPN1) to maximally 17 alanines. The disease is characterized by intranuclear deposits consisting primarily of PABPN1. In previous studies, we could show that the N-terminal domain of PABPN1 forms amyloid-like fibrils. Here, we analyze fibril formation of full-length PABPN1. Unexpectedly, fibril formation was independent of the presence of the alanine segment. With regard to fibril formation kinetics and resistance against denaturants, fibrils formed by full-length PABPN1 had completely different properties from those formed by the N-terminal domain. Fourier transformed infrared spectroscopy and limited proteolysis showed that fibrillar PABPN1 has a structure that differs from native PABPN1. Circumstantial evidence is presented that the C-terminal domain is involved in fibril formation. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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