The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone.

All major classes of protein chaperones, including DnaK (the Hsp70 eukaryotic equivalent) and GroEL (the Hsp60 eukaryotic equivalent) have been found in Escherichia coli. Molecular chaperones enhance the yields of correctly folded polypeptides by preventing aggregation and even by disaggregating cer...

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書誌詳細
出版年:	EMBO J
主要な著者:	Wawrzynow, A, Wojtkowiak, D, Marszalek, J, Banecki, B, Jonsen, M, Graves, B, Georgopoulos, C, Zylicz, M
フォーマット:	Artigo
言語:	Inglês
出版事項:	Nature Publishing Group 1995
主題:	Research Article
オンライン･アクセス:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC398286/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7743994/ https://ncbi.nlm.nih.govhttps://doi.org/10.1002/j.1460-2075.1995.tb07179.x
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The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone.

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