Assisted folding of D-glyceraldehyde-3-phosphate dehydrogenase by trigger factor

被引:57
作者
Huang, GC
Li, ZY
Zhou, JM
Fischer, G
机构
[1] Acad Sinica, Natl Lab Biomacromol, Inst Biophys, Beijing 100101, Peoples R China
[2] Max Planck Gesell Forsch Stelle Enzymol Prot Faltu, D-06120 Halle, Germany
关键词
chaperone; prolyl isomerase; protein folding; trigger factor;
D O I
10.1110/ps.9.6.1254
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The Escherichia coli trigger factor is a peptidyl-prolyl cis-trans isomerase that catalyzes proline-limited protein folding extremely well. Here. refolding of D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in the presence of trigger factor was investigated. The regain of activity of GAPDH was markedly increased by trigger factor after either long-or short-term denaturation, and detectable aggregation of GAPDH intermediates was prevented. In bath cases, time courses of refolding of GAPDH were decelerated by trigger factor. The reactivation yield of GAPDH showed a slow down-turn when molar ratios of trigger factor to GAPDH were above 5, due to tight binding between bigger factor and GAPDH intermediates. Such inactive bound GAPDH could be partially rescued from trigger factor by addition of reduced alpha LA as competitor, by further diluting the refolding mixture, or by disrupting hydrophobic interactions in the complexes. A model for trigger factor assisted refolding of GAPDH is proposed. We also suggest that assisted refolding nt GAPDH is due mainly to the chaperone function of trigger factor.
引用
收藏
页码:1254 / 1261
页数:8
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