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|Title:||The Machado-Joseph disease-associated expanded form of ataxin-3: overexpression, purification, and preliminary biophysical and structural characterization|
|Author:||Contessotto, Miriam G. G.|
Murai, Luciana K. Rosselli
Garcia, Maria Cristina C.
Oliveira, Cristiano L. P.
Torriani, Iris L.
Cendes, Iscia Lopes
Murai, Marcelo J.
|Abstract:||An expansion of the polyglutamine (polyQ) tract within the deubiquitinase ataxin-3 protein is believed to play a role in a neurodegenerative disorder. Ataxin-3 contains a Josephin catalytic domain and a polyQ tract that renders it intrinsically prone to aggregate, and thus full-length protein is difficult to characterize structurally by high-resolution methods. We established a robust protocol for expression and purification of wild-type and expanded ataxin-3, presenting 19Q and 74Q, respectively. Both proteins are monodisperse as assessed by analytical size exclusion chromatography. Initial biophysical characterization was performed, with apparent transition melting temperature of expanded ataxin-3 lower than the wild-type counterpart. We further characterize the molecular envelope of wild-type and expanded polyQ tract in ataxin-3 using small angle X-ray scattering (SAXS). Characterization of protein-protein interactions between ataxin-3 and newly identified binding partners will benefit from our protocol.|
Doença de Machado-Joseph
Espalhamento de raios-X a baixo ângulo
Small angle X ray scattering
|Appears in Collections:||IFGW - Artigos e Outros Documentos|
FCM - Artigos e Outros Documentos
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