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Unfolding the chaperone story

Protein folding in the cell was originally assumed to be a spontaneous process, based on Anfinsen’s discovery that purified proteins can fold on their own after removal from denaturant. Consequently cell biologists showed little interest in the protein folding process. This changed only in the mid a...

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Autor principal: Hartl, F. Ulrich
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5662250/
https://www.ncbi.nlm.nih.gov/pubmed/29084909
http://dx.doi.org/10.1091/mbc.E17-07-0480
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author Hartl, F. Ulrich
author_facet Hartl, F. Ulrich
author_sort Hartl, F. Ulrich
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description Protein folding in the cell was originally assumed to be a spontaneous process, based on Anfinsen’s discovery that purified proteins can fold on their own after removal from denaturant. Consequently cell biologists showed little interest in the protein folding process. This changed only in the mid and late 1980s, when the chaperone story began to unfold. As a result, we now know that in vivo, protein folding requires assistance by a complex machinery of molecular chaperones. To ensure efficient folding, members of different chaperone classes receive the nascent protein chain emerging from the ribosome and guide it along an ordered pathway toward the native state. I was fortunate to contribute to these developments early on. In this short essay, I will describe some of the critical steps leading to the current concept of protein folding as a highly organized cellular process.
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spelling pubmed-56622502018-01-16 Unfolding the chaperone story Hartl, F. Ulrich Mol Biol Cell ASCB Award Essays Protein folding in the cell was originally assumed to be a spontaneous process, based on Anfinsen’s discovery that purified proteins can fold on their own after removal from denaturant. Consequently cell biologists showed little interest in the protein folding process. This changed only in the mid and late 1980s, when the chaperone story began to unfold. As a result, we now know that in vivo, protein folding requires assistance by a complex machinery of molecular chaperones. To ensure efficient folding, members of different chaperone classes receive the nascent protein chain emerging from the ribosome and guide it along an ordered pathway toward the native state. I was fortunate to contribute to these developments early on. In this short essay, I will describe some of the critical steps leading to the current concept of protein folding as a highly organized cellular process. The American Society for Cell Biology 2017-11-01 /pmc/articles/PMC5662250/ /pubmed/29084909 http://dx.doi.org/10.1091/mbc.E17-07-0480 Text en © 2017 Hartl. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology.
spellingShingle ASCB Award Essays
Hartl, F. Ulrich
Unfolding the chaperone story
title Unfolding the chaperone story
title_full Unfolding the chaperone story
title_fullStr Unfolding the chaperone story
title_full_unstemmed Unfolding the chaperone story
title_short Unfolding the chaperone story
title_sort unfolding the chaperone story
topic ASCB Award Essays
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5662250/
https://www.ncbi.nlm.nih.gov/pubmed/29084909
http://dx.doi.org/10.1091/mbc.E17-07-0480
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