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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
2002-12-31
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pubmed:abstractText |
GroEL/S chaperonin ring complexes fold many unrelated proteins. To understand the basis and extent of the chaperonin substrate spectrum, we used rounds of selection and DNA shuffling to obtain GroEL/S variants that dramatically enhanced folding of a single substrate-green fluorescent protein (GFP). Changes in the substrate-optimized chaperonins increase the polarity of the folding cavity and alter the ATPase cycle. These findings reveal a surprising plasticity of GroEL/S, which can be exploited to aid folding of recombinant proteins. Our studies also reveal a conflict between specialization and generalization of chaperonins as increased GFP folding comes at the expense of the ability of GroEL/S to fold its natural substrates. This conflict and the nature of the ring structure may help explain the evolution of cellular chaperone systems.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
111
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1027-39
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12507429-Adenosine Triphosphatases,
pubmed-meshheading:12507429-Chaperonin 10,
pubmed-meshheading:12507429-Chaperonin 60,
pubmed-meshheading:12507429-Directed Molecular Evolution,
pubmed-meshheading:12507429-Escherichia coli,
pubmed-meshheading:12507429-Eukaryotic Cells,
pubmed-meshheading:12507429-Evolution, Molecular,
pubmed-meshheading:12507429-Gene Expression Regulation, Bacterial,
pubmed-meshheading:12507429-Green Fluorescent Proteins,
pubmed-meshheading:12507429-Luminescent Proteins,
pubmed-meshheading:12507429-Mutation,
pubmed-meshheading:12507429-Prokaryotic Cells,
pubmed-meshheading:12507429-Protein Folding,
pubmed-meshheading:12507429-Protein Isoforms
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pubmed:year |
2002
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pubmed:articleTitle |
Directed evolution of substrate-optimized GroEL/S chaperonins.
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pubmed:affiliation |
Howard Hughes Medical Institute and Department of Cellular and Molecular Pharmacology, University of California, San Francisco 94143, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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