Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/338022
Type: Artigo
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.
Subject: Ataxia
Doença de Machado-Joseph
Espalhamento de raios-X a baixo ângulo
Ataxia
Machado-Joseph disease
Small angle X ray scattering
Country: Estados Unidos
Editor: Academic Press
Rights: fechado
Identifier DOI: 10.1016/j.pep.2018.07.005
Address: https://www.sciencedirect.com/science/article/pii/S1046592818302432
Date Issue: 2018
Appears in Collections:IFGW - Artigos e Outros Documentos
FCM - Artigos e Outros Documentos

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