The effect of amino acid substitution in the imperfect repeat sequences of α-synuclein on fibrillation

Biochimica et Biophysica Acta - Molecular Basis of Disease

Volumn 1792, Issue 10, 2009, Pages 998-1003

  Harada, Ryuichi ^a   Kobayashi, Natsuki ^a   Kim, Jihoon ^a   Nakamura, Chikashi ^b   Han, Sung Woong ^b   Ikebukuro, Kazunori ^a   Sode, Koji ^a  

^a TOKYO UNIVERSITY OF AGRICULTURE AND TECHNOLOGY   (Japan)

^b NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

Author keywords

Synuclein; E46K; Fibrillation; Imperfect repeat sequences; Parkinson's disease

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID; GLUTAMINE; GLYCINE; LYSINE;

ALPHA HELIX; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; ATOMIC FORCE MICROSCOPY; CIRCULAR DICHROISM; CONTROLLED STUDY; DEGENERATIVE DISEASE; DIFFUSE LEWY BODY DISEASE; GENE MUTATION; MOLECULAR CLONING; NEUROFILAMENT; NUCLEOTIDE REPEAT; PARKINSON DISEASE; PATHOGENESIS; POINT MUTATION; PRIORITY JOURNAL; PROTEIN AGGREGATION;

ALPHA-SYNUCLEIN; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CIRCULAR DICHROISM; HUMANS; LIGHT; MICROSCOPY, ATOMIC FORCE; MOLECULAR SEQUENCE DATA; MUTANT PROTEINS; PROPANOLS; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; REPETITIVE SEQUENCES, AMINO ACID; SCATTERING, RADIATION;

EID: 70349290550     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbadis.2009.06.010     Document Type: Article

References (32)

1. Giasson B.I., Murray I.V., Trojanowski J.Q., and Lee V.M. A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly. J. Biol. Chem. 276 (2001) 2380-2386
2. Du H.N., Tang L., Luo X.Y., Li H.T., Hu J., Zhou J.W., and Hu H.Y. A peptide motif consisting of glycine, alanine, and valine is required for the fibrillization and cytotoxicity of human alpha-synuclein. Biochemistry 42 (2003) 8870-8878
3. Uversky V.N., and Fink A.L. Amino acid determinants of alpha-synuclein aggregation: putting together pieces of the puzzle. FEBS Lett. 522 (2002) 9-13
4. Sode K., Usuzaka E., Kobayashi N., and Ochiai S. Engineered alpha-synuclein prevents wild type and familial Parkin variant fibril formation. Biochem. Biophys. Res. Commun. 335 (2005) 432-436
5. Serpell L.C., Berriman J., Jakes R., Goedert M., and Crowther R.A. Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 4897-4902
6. George J.M., Jin H., Woods W.S., and Clayton D.F. Characterization of a novel protein regulated during the critical period for song learning in the zebra finch. Neuron 15 (1995) 361-372
7. Davidson W.S., Jonas A., Clayton D.F., and George J.M. Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes. J. Biol. Chem. 273 (1998) 9443-9449
8. Ulmer T.S., Bax A., Cole N.B., and Nussbaum R.L. Structure and dynamics of micelle-bound human alpha-synuclein. J. Biol. Chem. 280 (2005) 9595-9603
9. Bussell Jr. R., and Eliezer D. A structural and functional role for 11-mer repeats in alpha-synuclein and other exchangeable lipid binding proteins. J. Mol. Biol. 329 (2003) 763-778
10. Zhu M., and Fink A.L. Lipid binding inhibits alpha-synuclein fibril formation. J. Biol. Chem. 278 (2003) 16873-16877
11. Munishkina L.A., Phelan C., Uversky V.N., and Fink A.L. Conformational behavior and aggregation of alpha-synuclein in organic solvents: modeling the effects of membranes. Biochemistry 42 (2003) 2720-2730
12. Kessler J.C., Rochet J.C., and Lansbury Jr. P.T. The N-terminal repeat domain of alpha-synuclein inhibits beta-sheet and amyloid fibril formation. Biochemistry 42 (2003) 672-678
13. Sode K., Ochiai S., Kobayashi N., and Usuzaka E. Effect of reparation of repeat sequences in the human alpha-synuclein on fibrillation ability. Int. J. Biol. Sci. 3 (2007) 1-7
14. Polymeropoulos M.H., Lavedan C., Leroy E., Ide S.E., Dehejia A., Dutra A., Pike B., Root H., Rubenstein J., Boyer R., Stenroos E.S., Chandrasekharappa S., Athanassiadou A., Papapetropoulos T., Johnson W.G., Lazzarini A.M., Duvoisin R.C., Di Iorio G., Golbe L.I., and Nussbaum R.L. Mutation in the alpha-synuclein gene identified in families with Parkinson's disease. Science 276 (1997) 2045-2047
15. Kruger R., Kuhn W., Muller T., Woitalla D., Graeber M., Kosel S., Przuntek H., Epplen J.T., Schols L., and Riess O. Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease. Nat. Genet. 18 (1998) 106-108
16. Zarranz J.J., Alegre J., Gomez-Esteban J.C., Lezcano E., Ros R., Ampuero I., Vidal L., Hoenicka J., Rodriguez O., Atares B., Llorens V., Gomez Tortosa E., del Ser T., Munoz D.G., and de Yebenes J.G. The new mutation, E46K, of alpha-synuclein causes Parkinson and Lewy body dementia. Ann. Neurol. 55 (2004) 164-173
17. Choi W., Zibaee S., Jakes R., Serpell L.C., Davletov B., Crowther R.A., and Goedert M. Mutation E46K increases phospholipid binding and assembly into filaments of human alpha-synuclein. FEBS Lett. 576 (2004) 363-368
18. Greenbaum E.A., Graves C.L., Mishizen-Eberz A.J., Lupoli M.A., Lynch D.R., Englander S.W., Axelsen P.H., and Giasson B.I. The E46K mutation in alpha-synuclein increases amyloid fibril formation. J. Biol. Chem. 280 (2005) 7800-7807
19. Pandey N., Schmidt R.E., and Galvin J.E. The alpha-synuclein mutation E46K promotes aggregation in cultured cells. Exp. Neurol. 197 (2006) 515-520
20. Koo H.J., Lee H.J., and Im H. Sequence determinants regulating fibrillation of human alpha-synuclein. Biochem. Biophys. Res. Commun. 368 (2008) 772-778
21. Kobayashi M., Kim J., Kobayashi N., Han S., Nakamura C., Ikebukuro K., and Sode K. Pyrroloquinoline quinone (PQQ) prevents fibril formation of alpha-synuclein. Biochem. Biophys. Res. Commun. 349 (2006) 1139-1144
22. Fredenburg R.A., Rospigliosi C., Meray R.K., Kessler J.C., Lashuel H.A., Eliezer D., and Lansbury Jr. P.T. The impact of the E46K mutation on the properties of alpha-synuclein in its monomeric and oligomeric states. Biochemistry 46 (2007) 7107-7118
23. Uversky V.N., Li J., and Fink A.L. Evidence for a partially folded intermediate in alpha-synuclein fibril formation. J. Biol. Chem. 276 (2001) 10737-10744
24. Bertoncini C.W., Jung Y.S., Fernandez C.O., Hoyer W., Griesinger C., Jovin T.M., and Zweckstetter M. Release of long-range tertiary interactions potentiates aggregation of natively unstructured alpha-synuclein. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 1430-1435
25. Rospigliosi C.C., McClendon S., Schmid A.W., Ramlall T.F., Barre P., Lashuel H.A., and Eliezer D. E46K Parkinson's-linked mutation enhances C-terminal-to-N-terminal contacts in alpha-synuclein. J. Mol. Biol. 388 (2009) 1022-1032
26. Del Mar C., Greenbaum E.A., Mayne L., Englander S.W., and Woods Jr. V.L. Structure and properties of alpha-synuclein and other amyloids determined at the amino acid level. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 15477-15482
27. Heise H., Hoyer W., Becker S., Andronesi O.C., Riedel D., and Baldus M. Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 15871-15876
28. Chen M., Margittai M., Chen J., and Langen R. Investigation of alpha-synuclein fibril structure by site-directed spin labeling. J. Biol. Chem. 282 (2007) 24970-24979
29. Heise H., Celej M.S., Becker S., Riedel D., Pelah A., Kumar A., Jovin T.M., and Baldus M. Solid-state NMR reveals structural differences between fibrils of wild-type and disease-related A53T mutant alpha-synuclein. J. Mol. Biol. 380 (2008) 444-450
30. Zibaee S., Jakes R., Fraser G., Serpell L.C., Crowther R.A., and Goedert M. Sequence determinants for amyloid fibrillogenesis of human alpha-synuclein. J. Mol. Biol. 374 (2007) 454-464
31. Chien P., Weissman J.S., and DePace A.H. Emerging principles of conformation-based prion inheritance. Annu. Rev. Biochem. 73 (2004) 617-656
32. Nekooki-Machida Y., Kurosawa M., Nukina N., Ito K., Oda T., and Tanaka M. Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity. Proc. Natl. Acad. Sci. U. S. A. 106 (2009) 9679-9684