Oligoproline effects on polyglutamine conformation and aggregation

Journal of Molecular Biology

Volumn 355, Issue 3, 2006, Pages 524-535

  Bhattacharyya, Anusri ^a   Thakur, Ashwani K ^a   Chellgren, Veronique M ^b   Thiagarajan, Geetha ^a   Williams, Angela D ^a   Chellgren, Brian W ^b   Creamer, Trevor P ^b   Wetzel, Ronald ^a  

^a UNIVERSITY OF TENNESSEE GRADUATE SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF KENTUCKY   (United States)

Author keywords

Amyloid; Conformation; Huntington's disease; Oligoproline; Polyglutamine

Indexed keywords

AMYLOID; POLYGLUTAMINE; PROLINE;

ALPHA HELIX; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CORRELATION ANALYSIS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN STABILITY; PROTEIN STRUCTURE;

ANIMALIA;

EID: 28944446477     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.10.053     Document Type: Article

References (51)

1. G.P. Bates, and C. Benn The polyglutamine diseases G.P. Bates P.S. Harper L. Jones Huntington's Disease 2002 Oxford University Press Oxford, UK 429 472
2. E. Scherzinger, A. Sittler, K. Schweiger, V. Heiser, R. Lurz, and R. Hasenbank Self-assembly of polyglutamine-containing huntingtin fragments into amyloid-like fibrils: implications for Huntington's disease pathology Proc. Natl Acad. Sci. USA 96 1999 4604 4609
3. S. Chen, V. Berthelier, W. Yang, and R. Wetzel Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity J. Mol. Biol. 311 2001 173 182
4. M. Arrasate, S. Mitra, E.S. Schweitzer, M.R. Segal, and S. Finkbeiner Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death Nature 431 2004 805 810
5. H. Mukai, T. Isagawa, E. Goyama, S. Tanaka, N.F. Bence, and A. Tamura Formation of morphologically similar globular aggregates from diverse aggregation-prone proteins in mammalian cells Proc. Natl Acad. Sci. USA 102 2005 10887 10892
6. R. Wetzel Chemical and physical properties of polyglutamine repeat sequences R. Wells T. Ashizawa Genetic Instabilities and Neurological Diseases 2nd edit. 2005 Elsevier San Diego In the press
7. A.P. Osmand, V. Berthelier, and R. Wetzel Imaging polyglutamine deposits in brain tissue Methods Enzymol 2005 In the press
8. E.J. Slow, R.K. Graham, A.P. Osmand, R.S. Devon, G. Lu, and Y. Deng Absence of behavioral abnormalities and neurodegeneration in vivo despite widespread neuronal huntingtin inclusions Proc. Natl Acad. Sci. USA 102 2005 11402 11407
9. S. Chen, F. Ferrone, and R. Wetzel Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation Proc. Natl Acad. Sci. USA 99 2002 11884 11889
10. C.J. Cummings, M.A. Mancini, B. Antalffy, D.B. DeFranco, H.T. Orr, and H.Y. Zoghbi Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1 Nature Genet. 19 1998 148 154
11. Y. Chai, S.L. Koppenhafer, N.M. Bonini, and H.L. Paulson Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease J. Neurosci. 19 1999 10338 10347
12. J.M. Warrick, H.Y. Chan, G.L. Gray-Board, Y. Chai, H.L. Paulson, and N.M. Bonini Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70 Nature Genet. 23 1999 425 428
13. P. Kazemi-Esfarjani, and S. Benzer Genetic suppression of polyglutamine toxicity in Drosophila Science 287 2000 1837 1840
14. P. Venkatraman, R. Wetzel, M. Tanaka, N. Nukina, and A.L. Goldberg Eukaryotic proteasomes cannot digest polyglutamine sequences and release them intact during degradation of polyglutamine-containing proteins Mol. Cell 14 2004 95 104
15. S. Vigouroux, M. Briand, and Y. Briand Linkage between the proteasome pathway and neurodegenerative diseases and aging Mol. Neurobiol. 30 2004 201 221
16. L. Petrucelli, and T.M. Dawson Mechanism of neurodegenerative disease: role of the ubiquitin proteasome system Annu. Med. 36 2004 315 320
17. E. Scherzinger, R. Lurz, M. Turmaine, L. Mangiarini, B. Hollenbach, and R. Hasenbank Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo Cell 90 1997 549 558
18. M. DiFiglia, E. Sapp, K.O. Chase, S.W. Davies, G.P. Bates, J.P. Vonsattel, and N. Aronin Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain Science 277 1997 1990 1993
19. N. Aronin, M. Kim, G. Laforet, and M. DiFiglia Are there multiple pathways in the pathogenesis of Huntington's disease? Phil. Trans. Roy. Soc. ser. B 354 1999 995 1003
20. K. Nozaki, O. Onodera, H. Takano, and S. Tsuji Amino acid sequences flanking polyglutamine stretches influence their potential for aggregate formation Neuroreport 12 2001 3357 3364
21. S.J. Wood, R. Wetzel, J.D. Martin, and M.R. Hurle Prolines and amyloidogenicity in fragments of the Alzheimer's peptide β/A4 Biochemistry 34 1995 724 730
22. D.F. Moriarty, and D.P. Raleigh Effects of sequential proline substitutions on amyloid formation by human amylin20-29 Biochemistry 38 1999 1811 1818
23. A. Thakur, and R. Wetzel Mutational analysis of the structural organization of polyglutamine aggregates Proc. Natl Acad. Sci. USA 99 2002 17014 17019
24. A.D. Williams, E. Portelius, I. Kheterpal, J.T. Guo, K.D. Cook, Y. Xu, and R. Wetzel Mapping abeta amyloid fibril secondary structure using scanning proline mutagenesis J. Mol. Biol. 335 2004 833 842
25. H. Takano, and J.F. Gusella The predominantly HEAT-like motif structure of huntingtin and its association and coincident nuclear entry with dorsal, an NF-kB/Rel/dorsal family transcription factor BMC Neurosci. 3 2002 15
26. S. Chen, V. Berthelier, J.B. Hamilton, B. O'Nuallain, and R. Wetzel Amyloid-like features of polyglutamine aggregates and their assembly kinetics Biochemistry 41 2002 7391 7399
27. J.D. Harper, and P.T. Lansbury Jr Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins Annu. Rev. Biochem. 66 1997 385 407
28. R. Wetzel Protein folding and aggregation in the expanded polyglutamine repeat diseases J. Buchner T. Kiefhaber The Protein Folding Handbook-Part-I 2005 Wiley-VCH Weinheim
29. B. O'Nuallain, S. Shivaprasad, I. Kheterpal, and R. Wetzel Thermodynamics of Aβ(1-40) amyloid fibril formation Biochemistry 44 2005 12709 12718
30. R.W. Woody Circular dichroism Methods Enzymol. 246 1995 34 71
31. n-OH Int. J. Pept. Protein Res. 19 1982 94 101
32. T.P. Creamer Left-handed polyproline II helix formation is (very) locally driven Proteins: Struct. Funct. Genet. 33 1998 218 226
33. M.A. Kelly, B.W. Chellgren, A.L. Rucker, J.M. Troutman, M.G. Fried, A.F. Miller, and T.P. Creamer Host-guest study of left-handed polyproline II helix formation Biochemistry 40 2001 14376 14383
34. C.W. Johnson Analysis of circular dichroism spectra Methods Enzymol. 210 1992 426 447
35. A.E. Bevivino, and P.J. Loll An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel beta-fibrils Proc. Natl Acad. Sci. USA 98 2001 11955 11960
36. L. Masino, G. Kelly, K. Leonard, Y. Trottier, and A. Pastore Solution structure of polyglutamine tracts in GST-polyglutamine fusion proteins FEBS Letters 513 2002 267 272
37. M.J. Bennett, K.E. Huey-Tubman, A.B. Herr, A.P. West, S.A. Ross, and P.J. Bjorkman A linear lattice model for poly-glutamine in CAG expansion diseases Proc. Natl Acad. Sci. USA 99 2002 11634 11639
38. E.L. Altschuler, N.V. Hud, J.A. Mazrimas, and B. Rupp Random coil conformation for extended polyglutamine stretches in aqueous soluble monomeric peptides J. Pept. Res. 50 1997 73 75
39. H.A. Popiel, Y. Nagai, O. Onodera, T. Inui, N. Fujikake, and Y. Urade Disruption of the toxic conformation of the expanded polyglutamine stretch leads to suppression of aggregate formation and cytotoxicity Biochem. Biophys. Res. Commun. 317 2004 1200 1206
40. H. Reiersen, and A.R. Rees The hunchback and its neighbours: proline as an environmental modulator Trends Biochem. Sci. 26 2001 679 684
41. M.P. Hinderaker, and R.T. Raines An electronic effect on protein structure Protein Sci. 12 2003 1188 1194
42. A.L. Rucker, C.T. Pager, M.N. Campbell, J.E. Qualls, and T.P. Creamer Host-guest scale of left-handed polyproline II helix formation Proteins: Struct. Funct. Genet. 53 2003 68 75
43. A. Chakrabartty, T. Kortemme, and R.L. Baldwin Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions Protein Sci. 3 1994 843 852
44. A.P. Minton Implications of macromolecular crowding for protein assembly Curr. Opin. Struct. Biol. 10 2000 34 39
45. M.D. Shtilerman, T.T. Ding, and P.T. Lansbury Jr Molecular crowding accelerates fibrillization of alpha-synuclein: could an increase in the cytoplasmic protein concentration induce Parkinson's disease? Biochemistry 41 2002 3855 3860
46. S.J. Wood, W. Chan, and R. Wetzel Seeding of Aβ fibril formation is inhibited by all three isotypes of apolipoprotein E Biochemistry 35 1996 12623 12628
47. E.W. Blanch, L.A. Morozova-Roche, D.A. Cochran, A.J. Doig, L. Hecht, and L.D. Barron Is polyproline II helix the killer conformation? A Raman optical activity study of the amyloidogenic prefibrillar intermediate of human lysozyme J. Mol. Biol. 301 2000 553 563
48. F. Eker, K. Griebenow, and R. Schweitzer-Stenner Abeta(1-28) fragment of the amyloid peptide predominantly adopts a polyproline II conformation in an acidic solution Biochemistry 43 2004 6893 6898
49. J.S. Richardson, and D.C. Richardson Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation Proc. Natl Acad. Sci. USA 99 2002 2754 2759
50. W.C. Wigley, M.J. Corboy, T.D. Cutler, P.H. Thibodeau, J. Oldan, and M.G. Lee A protein sequence that can encode native structure by disfavoring alternate conformations Nature Struct. Biol. 9 2002 381 388
51. S. Chen, and R. Wetzel Solubilization and disaggregation of polyglutamine peptides Protein Sci. 10 2001 887 891