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Positive cooperativity in the functioning of molecular chaperone GroEL.

作者信息

Bochkareva E S, Lissin N M, Flynn G C, Rothman J E, Girshovich A S

机构信息

Institute of Protein Research, Academy of Sciences of Russia, Moscow Region.

出版信息

J Biol Chem. 1992 Apr 5;267(10):6796-800.

PMID:1348056
Abstract

In the presence of its partner, GroES, the tetradecameric molecular chaperone GroEL binds 14 ATP molecules, half of which are hydrolyzed in a cooperative manner. Moreover GroEL can bind, with a positive cooperativity, more than two molecules of nonfolded protein rhodanese. The role of the cooperative mechanism in the functioning of GroEL is discussed.

摘要

相似文献

1
Positive cooperativity in the functioning of molecular chaperone GroEL.
J Biol Chem. 1992 Apr 5;267(10):6796-800.
2
Cooperativity in ATP hydrolysis by GroEL is increased by GroES.GroES可增强GroEL水解ATP时的协同性。
FEBS Lett. 1991 Nov 4;292(1-2):254-8. doi: 10.1016/0014-5793(91)80878-7.
3
The formation of symmetrical GroEL-GroES complexes in the presence of ATP.在ATP存在的情况下对称GroEL - GroES复合物的形成。
FEBS Lett. 1994 May 30;345(2-3):181-6. doi: 10.1016/0014-5793(94)00432-3.
4
The lower hydrolysis of ATP by the stress protein GroEL is a major factor responsible for the diminished chaperonin activity at low temperature.应激蛋白GroEL在低温下对ATP的水解作用降低，这是导致伴侣蛋白活性在低温时下降的一个主要因素。
Cryobiology. 2000 Dec;41(4):319-23. doi: 10.1006/cryo.2000.2287.
5
Truncated GroEL monomer has the ability to promote folding of rhodanese without GroES and ATP.截短的GroEL单体能够在没有GroES和ATP的情况下促进硫氰酸酶的折叠。
FEBS Lett. 1993 Dec 27;336(2):363-7. doi: 10.1016/0014-5793(93)80838-l.
6
The chaperonin GroEL binds a polypeptide in an alpha-helical conformation.伴侣蛋白GroEL以α螺旋构象结合一条多肽。
Biochemistry. 1991 Jul 30;30(30):7359-62. doi: 10.1021/bi00244a001.
7
Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES.伴侣蛋白GroEL和GroES中核苷酸结合区域的鉴定。
Nature. 1993 Nov 18;366(6452):279-82. doi: 10.1038/366279a0.
8
The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.伴侣蛋白辅助蛋白质折叠过程中GroEL和GroES的反应循环。
Nature. 1993 Nov 18;366(6452):228-33. doi: 10.1038/366228a0.
9
Conditions for nucleotide-dependent GroES-GroEL interactions. GroEL14(groES7)2 is favored by an asymmetric distribution of nucleotides.核苷酸依赖性GroES-GroEL相互作用的条件。核苷酸的不对称分布有利于GroEL14(groES7)2的形成。
J Biol Chem. 1997 Oct 24;272(43):26999-7004. doi: 10.1074/jbc.272.43.26999.
10
Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis.伴侣蛋白作用机制：在没有ATP水解的情况下，GroES的结合与释放可驱动GroEL介导的蛋白质折叠。
EMBO J. 1996 Nov 15;15(22):6111-21.

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