Self-assembly and conformational heterogeneity of the AXH domain of ataxin-1: An unusual example of a chameleon fold

Biophysical Journal

Volumn 104, Issue 6, 2013, Pages 1304-1313

  De Chiara, Cesira ^a   Rees, Martin ^b   Menon, Raj P ^a   Pauwels, Kris ^a   Lawrence, Ceri ^a   Konarev, Petr V ^c   Svergun, Dmitri I ^c   Martin, Stephen R ^a   Chen, Yu Wai ^b   Pastore, Annalisa ^a  

^a NATIONAL INSTITUTE FOR MEDICAL RESEARCH   (United Kingdom)

^b KING'S COLLEGE LONDON   (United Kingdom)

^c EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 84877046409     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2013.01.048     Document Type: Article

References (33)

1. Orr, H. T., M. Y. Chung,., H. Y. Zoghbi. 1993. Expansion of an unstable trinucleotide CAG repeat in spinocerebellar ataxia type 1. Nat. Genet. 4:221-226. (Pubitemid 23205168)
2. Zoghbi, H. Y., and H. T. Orr. 2008. Pathogenic mechanisms of a polyglutamine-mediated neurodegenerative disease, spinocerebellar ataxia type 1. J. Biol. Chem. 284:7425-7429.
3. Matilla-Duenas, A., R. Goold, and P. Giunti. 2008. Clinical, genetic, molecular, and pathophysiological insights into spinocerebellar ataxia type 1. Cerebellum. 7:106-114.
4. Chiti, F., and C. M. Dobson. 2006. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75:333-366. (Pubitemid 44118036)
5. Soto, C., and L. D. Estrada. 2008. Protein misfolding and neurodegeneration. Arch. Neurol. 65:184-189. (Pubitemid 351240778)
6. Klement, I. A., P. J. Skinner,., H. T. Orr. 1998. Ataxin-1 nuclear localization and aggregation: role in polyglutamine-induced disease in SCA1 transgenic mice. Cell. 95:41-53. (Pubitemid 28458023)
7. Emamian, E. S., M. D. Kaytor,., H. T. Orr. 2003. Serine 776 of ataxin-1 is critical for polyglutamine-induced disease in SCA1 transgenic mice. Neuron. 38:375-387. (Pubitemid 36579141)
8. Masino, L., G. Nicastro,., A. Pastore. 2004. Characterization of the structure and the amyloidogenic properties of the Josephin domain of the polyglutamine-containing protein ataxin-3. J. Mol. Biol. 344: 1021-1035. (Pubitemid 39491247)
9. de Chiara, C., R. P. Menon,., A. Pastore. 2005. Polyglutamine is not all: the functional role of the AXH domain in the ataxin-1 protein. J. Mol. Biol. 354:883-893. (Pubitemid 41735509)
10. Tsuda, H., H. Jafar-Nejad,., H. Y. Zoghbi. 2005. The AXH domain of Ataxin-1 mediates neurodegeneration through its interaction with Gfi-1/Senseless proteins. Cell. 122:633-644. (Pubitemid 41191160)
11. Saunders, H. M., and S. P. Bottomley. 2009. Multi-domain misfolding: understanding the aggregation pathway of polyglutamine proteins. Protein Eng. Des. Sel. 22:447-451.
12. de Chiara, C., C. Giannini, A. Pastore. 2003. The AXH module: an independently folded domain common to ataxin-1 and HBP1. FEBS Lett. 551:107-112. (Pubitemid 37281336)
13. de Chiara, C., and A. Pastore. 2011. Polyglutamine Diseases and Neurodegeneration: The Example of Ataxin-1. In Supramolecular Structure and Function, Vol. 10. J. Brnjas-Kraljevi-c and G. Pifat-Mrzljak, editors. Springer, New York. 87-99.
14. Burright, E. N., J. D. Davidson,., H. T. Orr. 1997. Identification of a self-association region within the SCA1 gene product, ataxin-1. Hum. Mol. Genet. 6:513-518. (Pubitemid 27142099)
15. de Chiara, C., R. P. Menon,., A. Pastore. 2005. The AXH domain adopts alternative folds the solution structure of HBP1 AXH. Structure. 13:743-753. (Pubitemid 40704663)
16. Andreeva, A., and A. G. Murzin. 2006. Evolution of protein fold in the presence of functional constraints. Curr. Opin. Struct. Biol. 16:399-408. (Pubitemid 43831641)
17. Yeates, T. O. 2007. Protein structure: evolutionary bridges to new folds. Curr. Biol. 17:R48-R50. (Pubitemid 46107829)
18. Chen, Y. W., M. D. Allen,., M. Bycroft. 2004. The structure of the AXH domain of spinocerebellar ataxin-1. J. Biol. Chem. 279:3758-3765. (Pubitemid 38140620)
19. Powell, H. R. 1999. The Rossmann Fourier autoindexing algorithm in MOSFLM. Acta Crystallogr. D Biol. Crystallogr. 55:1690-1695. (Pubitemid 29504423)
20. Evans, P. E. 2006. Scaling and assessment of data quality. Acta Crystallogr. D Biol. Crystallogr. 62:72-82.
21. Strong, M., M. R. Sawaya,., D. Eisenberg. 2006. Toward the structural genomics of complexes: crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. ;USA. 103:8060-8065. (Pubitemid 43801052)
22. McCoy, A. J., R. W. Grosse-Kunstleve, R. J. Read. 2007. PHASER ;crystallographic software. J. Appl. Cryst. 40:658-674.
23. Adams, P. D., P. V. Afonine, P. H. Zwart. 2010. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66:213-221.
24. Emsley, P., B. Lohkamp,., K. Cowtan. 2010. Features and development of COOT. Acta Crystallogr. D Biol. Crystallogr. 66:486-501.
25. Painter, J., and E. A. Merritt. 2006. Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr. D Biol. Crystallogr. 62:439-450.
26. Davis, I.W., A. Leaver-Fay,., D. C. Richardson. 2007.MOLPROBITY: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res. 35(Web Server issue):W375-W383.
27. Roessle, M. W., R. Klaering,., D. Svergun. 2007. Upgrade of the small-angle x-ray scattering beamline X33 at the European Molecular Biology Laboratory, Hamburg. J. Appl. Cryst. 40:s190-s194. (Pubitemid 46732685)
28. Konarev, P. V., V. V. Volkov,., D. I. Svergun. 2003. PRIMUS: a Windows PC-based system for small-angle scattering data analysis. J. Appl. Cryst. 36:1277-1282.
29. Svergun, D. I. 1992. Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Cryst. 25:495-503. (Pubitemid 23564996)
30. Svergun, D., C. Barberato, and M. H. Koch. 1995. CRYSOL -A program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Cryst. 28:768-773. (Pubitemid 3014671)
31. Krissinel, E., and K. Henrick. 2007. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372:774-797. (Pubitemid 47321791)
32. Nooren, I. M., A. V. George,., R. Boelens. 1999. NMR structure determination of the tetramerization domain of the Mnt repressor: an asymmetric a-helical assembly in slow exchange. J. Biomol. NMR. 15:39-53. (Pubitemid 29488027)
33. Nooren, I. M., R. Kaptein,., R. Boelens. 1999. The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils. Nat. Struct. Biol. 6:755-759. (Pubitemid 29360237)