Chaperone-like activities of α-synuclein: α-Synuclein assists enzyme activities of esterases

Biochemical and Biophysical Research Communications

Volumn 346, Issue 4, 2006, Pages 1142-1149

  Ahn, Misun ^a   Kim, SeungBum ^a   Kang, Mira ^a   Ryu, Yeonwoo ^a   Doohun Kim, T ^a  

^a Ajou University   (South Korea)

Author keywords

Synuclein; Intrinsically unstructured; Microbial esterases

Indexed keywords

ALPHA SYNUCLEIN; CHAPERONE; ESTERASE;

ARTICLE; ATOMIC FORCE MICROSCOPY; CARBOXY TERMINAL SEQUENCE; CELL PH; CELL PROTECTION; COMPLEX FORMATION; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME CONFORMATION; ENZYME STABILITY; ENZYME STRUCTURE; HEAT; OXIDATIVE STRESS; PH MEASUREMENT; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; STRUCTURE ANALYSIS;

ALPHA-SYNUCLEIN; ENZYME STABILITY; ESTERASES; HUMANS; HYDROGEN-ION CONCENTRATION; LEWY BODIES; MICROSCOPY, ATOMIC FORCE; MOLECULAR CHAPERONES; PARKINSON DISEASE; SOLVENTS;

EID: 33745375279     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.05.213     Document Type: Article

References (27)

1. Bennett M.C. The role of alpha-synuclein in neurodegenerative diseases. Pharmacol. Ther. 105 (2005) 311-331
2. Sidhu A., Wersinger C., Moussa C.E.-H., and Vernier P. The role of {alpha}-synuclein in both neuroprotection and neurodegeneration. Ann. N. Y. Acad. Sci. 1035 (2004) 250-270
3. Golbe L.I. Alpha-synuclein and Parkinson's disease. Adv. Neurol. 91 (2003) 165-174
4. Vekrellis K., Rideout H.J., and Stefanis L. Neurobiology of alpha-synuclein. Mol. Neurobiol. 30 (2004) 1-21
5. Paleologou K.E., Irvine G.B., and El-Agnaf O.M. Alpha-synuclein aggregation in neurodegenerative diseases and its inhibition as a potential therapeutic strategy. Biochem. Soc. Trans. 33 (2005) 1106-1110
6. Hashimoto M., Hsu L.J., Xia Y., Takeda A., Sisk A., Sundsmo M., and Masliah E. Oxidative stress induces amyloid-like aggregate formation of NACP/alpha-synuclein in vitro. Neuroreport 10 (1999) 717-721
7. Paxinou E., Chen Q., Weisse M., Giasson B.I., Norris E.H., Rueter S.M., Trojanowski J.Q., Lee V.M., and Ischiropoulos H. Induction of alpha-synuclein aggregation by intracellular nitrative insult. J. Neurosci. 21 (2001) 8053-8061
8. Kim T.D., Choi E., Rhim H., Paik S.R., and Yang C.-H. Alpha-synuclein has structural and functional similarities to small heat shock proteins. Biochem. Biophys. Res. Commun. 324 (2004) 1352-1359
9. Souza J.M., Giasson B.I., Lee V.M., and Ischiropoulos H. Chaperone-like activity of synucleins. FEBS Lett. 474 (2000) 116-119
10. Kim T.D., Paik S.R., and Yang C.H. Structural and functional implications of C-terminal regions of alpha-synuclein. Biochemistry 41 (2002) 13782-13790
11. Fernandez C.O., Hoyer W., Zweckstetter M., Jares-Erijman E.A., Subramaniam V., Griesinger C., and Jovin T.M. NMR of alpha-synuclein-polyamine complexes elucidates the mechanism and kinetics of induced aggregation. EMBO J. 23 (2004) 2039-2046
12. Li W., West N., Colla E., Pletnikova O., Troncoso J.C., Marsh L., Dawson T.M., Jakala P., Hartmann T., Price D.L., and Lee M.K. Aggregation promoting C-terminal truncation of alpha-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations. Proc. Natl. Acad. Sci. USA 102 (2005) 2162-2167
13. Choi G.S., Kim J.Y., Kim J.H., Ryu Y.W., and Kim G.J. Construction and characterization of a recombinant esterase with high activity and enantioselectivity to (S)-ketoprofen ethyl ester. Protein Expr. Purif. 29 (2003) 85-93
14. Kim Y.J., Choi G.S., Kim S.B., Yoon G.S., Kim Y.S., and Ryu Y.W. Screening and characterization of a novel esterase from a metagenomic library. Protein Expr. Purif. 45 (2006) 315-323
15. Khalameyzer V., Fischer I., Bornscheuer U.T., and Altenbuchner J. Screening, nucleotide sequence, and biochemical characterization of an esterase from Pseudomonas fluorescens with high activity towards lactones. Appl. Environ. Microbiol. 65 (1999) 477-482
16. Miller R.B., and Karn R.C. A rapid spectrophotometric method for the determination of esterase activity. J. Biochem. Biophys. Methods 3 (1980) 345-354
17. Wei Y.J., Contreras A., Sheffield P., Osterlund T., Derewenda U., Kneusel R.E., Matern U., Holm C., and Derewenda Z.S. Crystal structure of brefeldin A esterase, a bacterial homolog of the mammalian hormone-sensitive lipase. Nat. Struct. Biol. 6 (1999) 340-345
18. Cygler M., and Schrag J.D. Structure as basis for understanding interfacial properties of lipases. Methods Enzymol. 284 (1997) 3-27
19. Weinreb P.H., Weiguo Z., Poon A.W., Conway K.A., and Lansbury P.T. NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry 35 (1996) 13709-13715
20. Lucking C.B., and Brice A. Alpha-synuclein and Parkinson's disease. Cell. Mol. Life Sci. 57 (2000) 1894-1908
21. Tompa P., and Csermely P. The role of structural disorder in the function of RNA and protein chaperones. FASEB J. 18 (2004) 1169-1175
22. Demchenko A.P. Recognition between flexible protein molecules: induced and assisted folding. J. Mol. Recogn. 14 (2001) 42-61
23. Hong W., Jiao W., Hu J., Zhang J., Liu C., Fu X., Shen D., Xia B., and Chang Z. Periplasmic protein HdeA exhibits chaperone-like activity exclusively within stomach pH range by transforming into disordered conformation. J. Biol. Chem. 280 (2005) 27029-27034
24. Chakrabarti A., Bhattacharya S., Ray S., and Bhattacharyya M. Binding of a denatured heme protein and ATP to erythroid spectrin. Biochem. Biophys. Res. Commun. 282 (2001) 1189-1193
25. Bhattacharyya M., Ray S., Bhattacharya S., and Chakrabarti A. Chaperone activity and prodan binding at the self-associating domain of erythroid spectrin. J. Biol. Chem. 279 (2004) 55080-55088
26. Bhattacharyya J., and Das K.P. Molecular chaperone-like properties of an unfolded protein, alpha(s)-casein. J. Biol. Chem. 274 (1999) 15505-15509
27. Dyson H.J., and Wright P.E. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 6 (2005) 197-208