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Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES.

作者信息

Peralta D, Hartman D J, Hoogenraad N J, Høj P B

机构信息

Department of Biochemistry, La Trobe University, Bundoora, Victoria, Australia.

出版信息

FEBS Lett. 1994 Feb 14;339(1-2):45-9. doi: 10.1016/0014-5793(94)80381-1.

DOI:10.1016/0014-5793(94)80381-1
PMID:7906229
Abstract

Pig heart mitochondrial malate dehydrogenase was chemically denatured in guanidine HCl. Upon 50-fold dilution of the denaturant spontaneous refolding could be observed in the temperature range 12-32 degrees C. At 36 degrees C spontaneous refolding was not observed but a stable folding intermediate that is fairly resistant to aggregation was formed. This intermediate is readily refolded by the chaperonins GroEL and GroES and may prove useful in future attempts to describe several aspects of chaperonin action at physiological temperatures.

摘要

相似文献

1
Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES.
FEBS Lett. 1994 Feb 14;339(1-2):45-9. doi: 10.1016/0014-5793(94)80381-1.
2
Escherichia coli chaperonins cpn60 (groEL) and cpn10 (groES) do not catalyse the refolding of mitochondrial malate dehydrogenase.大肠杆菌伴侣蛋白cpn60(groEL)和cpn10(groES)不能催化线粒体苹果酸脱氢酶的重折叠。
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3
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4
Refolding and recognition of mitochondrial malate dehydrogenase by Escherichia coli chaperonins cpn 60 (groEL) and cpn10 (groES).大肠杆菌伴侣蛋白cpn 60(groEL)和cpn10(groES)对线粒体苹果酸脱氢酶的重折叠与识别
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Minimal and optimal mechanisms for GroE-mediated protein folding.GroE介导蛋白质折叠的最小和最佳机制
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Influence of the GroE molecular chaperone machine on the in vitro refolding of Escherichia coli beta-galactosidase.GroE分子伴侣机器对大肠杆菌β-半乳糖苷酶体外重折叠的影响。
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Assay of malate dehydrogenase. A substrate for the E. coli chaperonins GroEL and GroES.苹果酸脱氢酶测定。大肠杆菌伴侣蛋白GroEL和GroES的一种底物。
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Chaperonin GroE and ADP facilitate the folding of various proteins and protect against heat inactivation.伴侣蛋白GroE和二磷酸腺苷(ADP)促进多种蛋白质的折叠,并防止其因受热而失活。
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Purification and characterization of chaperonin 60 and chaperonin 10 from the anaerobic thermophile Thermoanaerobacter brockii.来自嗜热厌氧杆菌的伴侣蛋白60和伴侣蛋白10的纯化与特性分析
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Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese.伴侣蛋白促进单体线粒体硫氰酸酶的体外折叠。
J Biol Chem. 1991 Jul 15;266(20):13044-9.

引用本文的文献

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LON is the master protease that protects against protein aggregation in human mitochondria through direct degradation of misfolded proteins.LON是主要蛋白酶,通过直接降解错误折叠的蛋白质来防止人类线粒体中的蛋白质聚集。
Sci Rep. 2015 Dec 2;5:17397. doi: 10.1038/srep17397.
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GroEL-mediated protein folding: making the impossible, possible.
GroEL介导的蛋白质折叠:化不可能为可能。
Crit Rev Biochem Mol Biol. 2006 Jul-Aug;41(4):211-39. doi: 10.1080/10409230600760382.
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Amide hydrogen exchange shows that malate dehydrogenase is a folded monomer at pH 5.酰胺氢交换表明,苹果酸脱氢酶在pH 5时是一种折叠的单体。
Protein Sci. 2001 May;10(5):1079-83. doi: 10.1110/ps.53201.
5
Chaperonin-assisted folding of glutamine synthetase under nonpermissive conditions: off-pathway aggregation propensity does not determine the co-chaperonin requirement.伴侣蛋白在非允许条件下协助谷氨酰胺合成酶折叠:偏离途径的聚集倾向并不决定共伴侣蛋白的需求。
Protein Sci. 2000 Dec;9(12):2405-12. doi: 10.1110/ps.9.12.2405.
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Recognition of partially-folded mitochondrial malate dehydrogenase by GroEL. Steady and time-dependent emission anisotropy measurements.GroEL对部分折叠的线粒体苹果酸脱氢酶的识别。稳态和时间依赖性发射各向异性测量。
Protein Sci. 1998 Dec;7(12):2587-94. doi: 10.1002/pro.5560071212.
7
GroEL-GroES-mediated protein folding requires an intact central cavity.伴侣蛋白GroEL- GroES介导的蛋白质折叠需要完整的中央腔。
Proc Natl Acad Sci U S A. 1998 Oct 13;95(21):12163-8. doi: 10.1073/pnas.95.21.12163.
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Phospholipid-assisted protein folding: phosphatidylethanolamine is required at a late step of the conformational maturation of the polytopic membrane protein lactose permease.磷脂辅助的蛋白质折叠:多跨膜蛋白乳糖通透酶构象成熟的后期步骤需要磷脂酰乙醇胺。
EMBO J. 1998 Sep 15;17(18):5255-64. doi: 10.1093/emboj/17.18.5255.
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Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60.伴侣蛋白10介导对伴侣蛋白60的ATP水解抑制作用的意义。
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The effect of macromolecular crowding on chaperonin-mediated protein folding.大分子拥挤对伴侣蛋白介导的蛋白质折叠的影响。
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