Chaperone-like activities of {alpha}-synuclein: {alpha}-Synuclein assists enzyme activities of esterases

{alpha}-Synuclein, a major constituent of Lewy bodies (LBs), has been implicated to play a critical role in the pathogenesis of Parkinson's disease (PD), although the physiological function of {alpha}-synuclein has not yet been known. Here we have shown that {alpha}-synuclein, which has no well...

Full description

Saved in:
Bibliographic Details
Published in:Biochemical and biophysical research communications 2006-08, Vol.346 (4)
Main Authors: Ahn, Misun, Kim, SeungBum, Kang, Mira, Ryu, Yeonwoo, Doohun Kim, T.
Format: Article
Language:English
Subjects:
60 APPLIED LIFE SCIENCES
ATOMIC FORCE MICROSCOPY
BIOLOGICAL STRESS
ENZYME ACTIVITY
ESTERASES
FLEXIBILITY
HEAT
IN VITRO
IN VIVO
NERVOUS SYSTEM DISEASES
ORGANIC SOLVENTS
PATHOGENESIS
PH VALUE
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:{alpha}-Synuclein, a major constituent of Lewy bodies (LBs), has been implicated to play a critical role in the pathogenesis of Parkinson's disease (PD), although the physiological function of {alpha}-synuclein has not yet been known. Here we have shown that {alpha}-synuclein, which has no well-defined secondary or tertiary structure, can protect the enzyme activity of microbial esterases against stress conditions such as heat, pH, and organic solvents. In particular, the flexibility of {alpha}-synuclein and its C-terminal region seems to be important for complex formation, but the structural integrity of the C-terminal region may not be required for stabilization of enzyme activity. In addition, atomic force microscopy (AFM) and in vivo enzyme assays showed highly specific interactions of esterases with {alpha}-synuclein. Our results indicate that {alpha}-synuclein not only protects the enzyme activity of microbial esterases in vitro, but also can stabilize the active conformation of microbial esterases in vivo.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2006.05.213