The 69 kDa Escherichia coli maltodextrin glucosidase does not get encapsulated underneath GroES and folds through trans mechanism during GroEL/ GroES‐assisted folding
The 69 kDa Escherichia coli maltodextrin glucosidase does not get encapsulated underneath GroES and folds through trans mechanism during GroEL/ GroES‐assisted folding
复制标题
69 kDa 大肠杆菌麦芽糖糊精葡萄糖苷酶不会被封装在 GroES 下，而是在 GroEL/ GroES 辅助折叠过程中通过反式机制折叠
DOI：
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发表时间：
2007
期刊：
影响因子：
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通讯作者：
T. Chaudhuri
中科院分区：
文献类型：
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作者：
S. Paul;Chanpreet Singh;S. Mishra;T. Chaudhuri
大肠杆菌伴侣蛋白GroEL和GroES利用顺式机制，在分子质量为~50 kDa的范围内，协助多种底物蛋白折叠，但关于它们如何协助较大蛋白质折叠的信息有限。考虑到GroEL的中心空腔可以容纳~60 kDa的非天然蛋白，研究GroEL - GroES辅助折叠足够大的底物蛋白以进行顺式封装是很重要的。在这项研究中，我们报道了GroEL/ GroES‐辅助69 kDa单片段大肠杆菌蛋白麦芽糊精葡萄糖苷酶（MalZ）在体内和体外折叠的机制。GroEL和GroES在大肠杆菌中的共表达导致体内外源性MalZ活性增强2倍。在体外实验中，ATP存在下的GroEL和GroES可使MalZ再折叠增强7倍。存在或不存在ATP的GroEL和单环GroEL （SR1）都不能增强MalZ的体外折叠。GroES不能封装GroEL绑定的MalZ。所有这些实验结果表明，GroEL/GroES辅助的MalZ折叠遵循反式机制，而变性MalZ和GroES结合在GroEL分子的相反环上。-Paul， S., Singh， C., Mishra， S., Chaudhuri， T. K.在GroEL/GroES辅助折叠过程中，69 kDa大肠杆菌麦芽糊精葡萄糖苷酶不会被包裹在GroES下面，并通过反式机制折叠。中华医学杂志，21(2007):2874-2885。
Escherichia coli chaperonin GroEL and GroES assist in folding of a wide variety of substrate proteins in the molecular mass range of ~50 kDa, using cis mechanism, but limited information is available on how they assist in folding of larger proteins. Considering that the central cavity of GroEL can accommodate a non‐native protein of ~60 kDa, it is important to study the GroEL‐GroES‐assisted folding of substrate proteins that are large enough for cis encapsulation. In this study, we have reported the mechanism of GroEL/ GroES‐assisted in vivo and in vitro folding of a 69 kDa monomelic E. coli protein maltodextrin glucosidase (MalZ). Coexpression of GroEL and GroES in E. coli causes a 2‐fold enhancement of exogenous MalZ activity in vivo. In vitro, GroEL and GroES in the presence of ATP give rise to a 7‐fold enhancement in MalZ refolding. Neither GroEL nor single ring GroEL (SR1) in the presence or absence of ATP could enhance the in vitro folding of MalZ. GroES could not encapsulate GroEL‐bound MalZ. All these experimental findings suggested that GroEL/GroES‐assisted folding of MalZ followed trans mechanism, whereas denatured MalZ and GroES bound to the opposite rings of a GroEL molecule.—Paul, S., Singh, C., Mishra, S., Chaudhuri, T. K. The 69 kDa Escherichia coli maltodextrin glucosidase does not get encapsulated underneath GroES and folds through trans mechanism during GroEL/GroES‐assisted folding. FASEB J. 21, 2874–2885 (2007)
通过 GroEL/ES 将不耐热折叠中间体选择性体内拯救为噬菌体 P22 结构蛋白。
DOI：
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发表时间：
1994
期刊：
The Journal of biological chemistry
影响因子：
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作者：
Gordon,CL;Sather,SK;Casjens,S;King,J
通讯作者：
King,J
大肠杆菌的 malZ 基因是麦芽糖调节子的成员，编码麦芽糖糊精葡萄糖苷酶。
DOI：
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发表时间：
1991
期刊：
The Journal of biological chemistry
影响因子：
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作者：
Tapio,S;Yeh,F;Shuman,HA;Boos,W
通讯作者：
Boos,W