Alpha-synuclein has structural and functional similarities to small heat shock proteins.
The aggregation and fibrillization of alpha-synuclein, a major component of Lewy bodies, is a key event in Parkinson's disease. Although the mechanisms of fibrils formation are largely investigated, physiological function of alpha-synuclein is not yet clearly elucidated. Here, we showed that C-terminal region of alpha-synuclein is similar to alpha-crystalline domain of small heat shock proteins. In our experiments, alpha-synuclein, like small heat shock proteins, protected cellular proteins from denaturation, and confer Escherichia coli cellular tolerances against thermal- and oxidative-stresses.
Kim
Thomas Doohun
TD
School of Chemistry and Molecular Engineering, Seoul National University, Seoul, Republic of Korea.
Choi
Eunjin
E
Rhim
Hyangshuk
H
Paik
Seung R
SR
Yang
Chul-Hak
CH
D048948:14-3-3 Proteins / Q000737:chemistry; D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry; D003080:Cold Temperature; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000378:metabolism*; D006358:Hot Temperature; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology*; D018384:Oxidative Stress; D016415:Sequence Alignment; D051843:Synucleins; D038201:alpha-Crystallins / Q000737:chemistry; D051844:alpha-Synuclein
D048948:14-3-3 Proteins; D019843:Archaeal Proteins; C113795:HSP16.5 protein, Methanococcus jannaschii; D006360:Heat-Shock Proteins; D009419:Nerve Tissue Proteins; D051843:Synucleins; D038201:alpha-Crystallins; D051844:alpha-Synuclein