Literature DB >> 14661975

Temperature-dependent, irreversible formation of amyloid fibrils by a soluble human ataxin-3 carrying a moderately expanded polyglutamine stretch (Q36).

Erlet Shehi1, Paola Fusi, Francesco Secundo, Sabrina Pozzuolo, Aurelio Bairati, Paolo Tortora.   

Abstract

The protein ataxin-3 is responsible for Machado-Joseph disease/spinocerebellar ataxia type 3, a neurodegenerative disorder caused by the presence of an expanded polyglutamine tract. A previous investigation [Bevivino, A. E., and Loll, P. J. (2001) Proc. Natl. Acad. Sci. U.S.A. 98, 11955-11960] showed that a nonexpanded ataxin-3 (Q27) was fully soluble, whereas an expanded form (Q78) gave rise to amyloid fibrils. Here, we report investigations on three forms of ataxin-3 (i.e., human nonexpanded (Q26), moderately expanded (Q36) ataxins-3, and the murine protein (Q6)). Far-UV circular dichroism spectra at room temperature were substantially similar, with a relatively high helical content. On heating to 96 degrees C, human Q26 and murine proteins did not display large structural changes, nor did they undergo any precipitation, which highlights their amazing heat-resistance. In contrast, human Q36 ataxin-3 underwent a progressive increase in the beta-sheet and a concomitant decrease in helical content when the temperature was shifted from 37 to 80 degrees C, followed by the irreversible formation of aggregates above 80 degrees C. They were shown to consist of amyloid fibrils, as supported by both electron microscopy images and the typical spectral shift displayed by Congo red when it was added to the protein at growing temperatures. We also found that protein precipitation could be prevented by mixing the dye with Q36 ataxin-3 prior to heating, which also confirms that the precipitates do represent authentic amyloid fibrils. In contrast, other compounds structurally related to Congo red did not exert significant effects. Our observations suggest that the temperature of the observed transition is inversely related to the length of the expansion. Finally, we suggest that antiamyloidogenic compounds might be selected on the basis of their ability to block or retard human Q36 ataxin-3 precipitation on heat-treatment.

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Year:  2003        PMID: 14661975     DOI: 10.1021/bi0352825

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


  10 in total

1.  Deubiquitinating function of ataxin-3: insights from the solution structure of the Josephin domain.

Authors:  Yuxin Mao; Francesca Senic-Matuglia; Pier Paolo Di Fiore; Simona Polo; Michael E Hodsdon; Pietro De Camilli
Journal:  Proc Natl Acad Sci U S A       Date:  2005-08-23       Impact factor: 11.205

2.  Interaction of selected divalent metal ions with human ataxin-3 Q36.

Authors:  Iwona Stawoska; Aleksandra Wesełucha-Birczyńska; Maria Elena Regonesi; Matteo Riva; Paolo Tortora; Grazyna Stochel
Journal:  J Biol Inorg Chem       Date:  2009-07-04       Impact factor: 3.358

3.  Physiological temperature has a crucial role in amyloid β in the absence and presence of hydrophobic and hydrophilic nanoparticles.

Authors:  Mahdi Ghavami; Meisam Rezaei; Reza Ejtehadi; Mina Lotfi; Mohammad A Shokrgozar; Baharak Abd Emamy; Jens Raush; Morteza Mahmoudi
Journal:  ACS Chem Neurosci       Date:  2012-12-14       Impact factor: 4.418

4.  A major role for side-chain polyglutamine hydrogen bonding in irreversible ataxin-3 aggregation.

Authors:  Antonino Natalello; Anna Maria Frana; Annalisa Relini; Alessandra Apicella; Gaetano Invernizzi; Carlo Casari; Alessandra Gliozzi; Silvia Maria Doglia; Paolo Tortora; Maria Elena Regonesi
Journal:  PLoS One       Date:  2011-04-13       Impact factor: 3.240

5.  Functional interactions as a survival strategy against abnormal aggregation.

Authors:  Laura Masino; Giuseppe Nicastro; Lesley Calder; Michele Vendruscolo; Annalisa Pastore
Journal:  FASEB J       Date:  2010-09-01       Impact factor: 5.191

6.  The Toxic Effects of Pathogenic Ataxin-3 Variants in a Yeast Cellular Model.

Authors:  Marcella Bonanomi; Cristina Visentin; Gaetano Invernizzi; Paolo Tortora; Maria Elena Regonesi
Journal:  PLoS One       Date:  2015-06-08       Impact factor: 3.240

7.  Pathological ATX3 Expression Induces Cell Perturbations in E. coli as Revealed by Biochemical and Biophysical Investigations.

Authors:  Diletta Ami; Barbara Sciandrone; Paolo Mereghetti; Jacopo Falvo; Tiziano Catelani; Cristina Visentin; Paolo Tortora; Salvador Ventura; Antonino Natalello; Maria Elena Regonesi
Journal:  Int J Mol Sci       Date:  2021-01-19       Impact factor: 5.923

8.  The relationship between aggregation and toxicity of polyglutamine-containing ataxin-3 in the intracellular environment of Escherichia coli.

Authors:  Gaetano Invernizzi; Francesco A Aprile; Antonino Natalello; Andrea Ghisleni; Amanda Penco; Annalisa Relini; Silvia M Doglia; Paolo Tortora; Maria E Regonesi
Journal:  PLoS One       Date:  2012-12-14       Impact factor: 3.240

9.  Conformational behavior and aggregation of ataxin-3 in SDS.

Authors:  Helen M Saunders; Victoria A Hughes; Roberto Cappai; Stephen P Bottomley
Journal:  PLoS One       Date:  2013-07-22       Impact factor: 3.240

Review 10.  Misfolding of amyloidogenic proteins and their interactions with membranes.

Authors:  Annalisa Relini; Nadia Marano; Alessandra Gliozzi
Journal:  Biomolecules       Date:  2013-12-27
  10 in total

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