Deamidation of α-synuclein

Protein Science

Volumn 18, Issue 8, 2009, Pages 1766-1773

  Robinson, Noah E ^a   Robinson, Matthew L ^a   Schulze, Stephanie E S ^b   Lai, Bert T ^b   Gray, Harry B ^b  

^a Oregon Institute of Science and Medicine   (United States)

^b California Institute of Technology   (United States)

Author keywords

synuclein; Deamidation; Fourier transform mass spectrometry; Proteins

Indexed keywords

ALPHA SYNUCLEIN; ASPARAGINE; DODECYL SULFATE SODIUM; MUTANT PROTEIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANALYTIC METHOD; ARTICLE; COLLISIONALLY ACTIVATED DISSOCIATION; DEAMINATION; HALF LIFE TIME; ION CYCLOTRON RESONANCE MASS SPECTROMETRY; MEASUREMENT; MICELLE; PRIORITY JOURNAL; PROTEIN BINDING; QUANTITATIVE ANALYSIS;

ALPHA-SYNUCLEIN; AMIDES; AMINO ACID SEQUENCE; ASPARAGINE; HUMANS; MOLECULAR SEQUENCE DATA; RECOMBINANT PROTEINS; SODIUM DODECYL SULFATE;

EID: 67749120314     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.183     Document Type: Article

References (28)

1. Uversky VN, Fink AL (2004) Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim Biophys Acta 1698:131-153.
2. Tollefsbol TO, Gracy RW (1983) Premature aging diseases-cellular and molecular-changes. Bioscience 33:634-639.
3. Jao CC, Der-Sarkisssian A, Chen J, Langen R (2004) Structure of membrane-bound alpha-synuclein studied by site-directed spin labeling. Proc Natl Acad Sci USA 101:8331-8336.
4. Lee JC, Langen R, Hummel PA, Gray HB, Winkler JR (2004) Alpha-synuclein structures from fluorescence energy-transfer kinetics: implications for the role of the protein in Parkinson's disease. Proc Natl Acad Sci USA 101:16466-16471.
5. Ulmer TS, Bax A, Cole NB, Nussbaum RL (2005) Structure and dynamics of micelle-bound human alpha-synuclein. J Biol Chem 280:9595-9603.
6. Polverino de Laureto P, Tosatto L, Frare E, Marin O, Uversky VN, Fontana A (2006) Conformational properties of the SDS-bound state of synuclein probed by limited proteolysis: unexpected rigidity of the acidic C-terminal tail. Biochemistry 45:11523-11531.
7. Tamamizu-Kato S, Kosaraju MG, Kato H, Raussens V, Ruysschaert JM, Narayanaswami V (2006) Calcium-triggered membrane interaction of the alpha-synuclein acidic tail. Biochemistry 45:10947-10956.
8. Robinson NE, Robinson AB (2004) Molecular clocks - deamidation of asparaginyl and glutaminyl residues in peptides and proteins. Althouse Press, Cave Junction, OR.
9. Robinson NE, Robinson AB (2008) Use of merrifield solid phase peptide synthesis in investigations of biological deamidation of peptides and proteins. Biopolymers 90:297-306.
10. Robinson NE, Robinson AB (2001) Molecular clocks. Proc Natl Acad Sci USA 98:944-949.
11. Robinson NE, Robinson AB, Merrifield RB (2001) Mass spectrometric evaluation of synthetic peptides as primary-structure models for peptide and protein deamidation. J Pept Protein Res 57:1-12.
12. Robinson NE, Robinson ZW, Robinson BR, Robinson AL, Robinson JA, Robinson ML, Robinson AB (2004) Structure-dependent nonenzymatic deamidation of glutaminyl and asparaginyl pentapeptides. J Pept Res 63:483-493.
13. Robinson NE, Robinson AB (2004) Prediction of primary-structure deamidation rates of asparaginyl and glutaminyl peptides through steric and catalytic effects. J Pept Res 63:437-448.
14. Robinson NE (2002) Protein deamidation. Proc Natl Acad Sci USA 99:5283-5288.
15. Robinson AB, McKerrow JH, Cary P (1970) Controlled deamidation of peptides and proteins-an experimental hazard and a possible biological timer. Proc Natl Acad Sci USA 66:753-757.
16. Nilsson MR, Driscoll M, Raleigh DP (2002) Low levels of asparagine deamidation can have a dramatic effect on aggregation of amyloidogenic peptides: implications for the study of amyloid formation. Protein Sci 11:342-349.
17. Yagi H, Kusaka E, Hongo K, Mizobata T, Kawata Y (2005) Amyloid fibril formation of alpha-synuclein is accelerated by preformed amyloid seeds of other proteins - implications for the mechanism of transmissible conformational diseases. J Biol Chem 280:38609-38616.
18. Robinson NE, Zabrouskov V, Zhang J, Lampi KJ, Robinson AB (2006) Measurement of deamidation of intact proteins by isotopic envelope and mass defect with ion cyclotron resonance Fourier transform mass spectrometry. Rapid Commun Mass Spectrom 20:3535-3541.
19. Robinson NE, Lampi KJ, McIver RT, Williams RH, Kruppa G, Robinson AB (2005) Quantitative measurement of deamidation in lens betaB2-crystallin and peptides by direct electrospray injection and fragmentation in a Fourier transform mass spectrometer. Mol Vis 11:1211-1219.
20. Zabrouskov V, Han X, Welker E, Zhai H, Lin C, Van Wijk KJ, Scheraga HA, McLafferty FW (2006) Stepwise deamidation of ribonuclease A at five sites determined by top down mass spectrometry. Biochemistry 45:987-992.
21. Robinson NE, Robinson AB (2001) Prediction of protein deamidation rates from primary and three-dimensional structure. Proc Natl Acad Sci USA 98:4367-4372.
22. Cappasso S, Salvadori S (1999) Effect of the three-dimensional structure on the deamidation reaction of ribonuclease A. J Pept Res 54:377-382.
23. Wearne SJ, Creighton TE (1989) Effect of protein conformation on rate of deamidation - ribonuclease A. Proteins 5:8-12.
24. Jakes R, Spillantini MG, Goedert M (1994) Identification of 2 distinct synucleins from human brain. FEBS Lett 345:27-32.
25. Jao CC, Der-Sarkissian A, Chen J, Langen R (2004) Structure of membrane-bound alpha-synuclein studied by site-directed spin labeling. Proc Natl Acad Sci USA 101:8331-8336.
26. Esposito C, Colicchio P, Facchiano A, Ragone R (1998) Effect of a weak electrolyte on the critical micellar concentration of sodium dodecyl sulfate. J Colloid Interface Sci 200:310-312.
27. Coplen TB, Böhlke JK, De Bièvre P, Ding T, Holden NE, Hopple JA, Krouse HR, Lamberty A, Peiser HS, Rèvèsz K, Rieder SE, Rosman KJR, Roth E, Taylor PDP, Vocke RD, Jr, Xiao YK (2002) Isotope-abundance variations of selected elements (IUPAC Technical Report). Pure Appl Chem 74:1987-2017.
28. Thannhauser TW, Scheraga HA (1985) Reversible blocking of half-cystine residues of proteins and an irreversible specific deamidation of asparagine-67 of S-sulforibonuclease under mild conditions. Biochemistry 24:7681-7668.