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  Functional significance of symmetrical versus asymmetrical groel-groes chaperonin complexes

Engel, A., Hayerhartl, M. K., Goldie, K. N., Pfeifer, G., Hegerl, R., Müller, S., et al. (1995). Functional significance of symmetrical versus asymmetrical groel-groes chaperonin complexes. Science, 269(5225), 832-836.

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Engel, A., Author
Hayerhartl, M. K., Author
Goldie, K. N., Author
Pfeifer, G.1, Author              
Hegerl, R.1, Author              
Müller, S.1, Author              
Dasilva, A. C. R., Author
Baumeister, W.1, Author              
Hartl, F. U.1, Author              
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1External Organizations, ou_persistent22              

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Free keywords: Escherichia-coli; Electron-microscopy; Central cavity; Protein; Hydrolysis; Surface; Binding.; Multidisciplinary. Multidisciplinary. Multidisciplinary.
 Abstract: The Escherichia coli chaperonin GroEL and its regulator GroES are thought to mediate adenosine triphosphate-dependent protein folding as an asymmetrical complex, with substrate protein bound within the GroEL cylinder. In contrast, a symmetrical complex formed between one GroEL and two GroES oligomers, with substrate protein binding to the outer surface of GroEL, was recently proposed to be the functional chaperonin unit. Electron microscopic and biochemical analyses have now shown that unphysiologically high magnesium concentrations and increased pH are required to assemble symmetrical complexes, the formation of which precludes the association of unfolded polypeptide. Thus, the functional significance of GroEL:(GroES)(2) particles remains to be demonstrated. [References: 31]

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 Dates: 1995-08-11
 Publication Status: Published in print
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 Identifiers: eDoc: 318418
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Title: Science
Source Genre: Journal
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Pages: - Volume / Issue: 269 (5225) Sequence Number: - Start / End Page: 832 - 836 Identifier: -