Abstract
We discuss recent experiments that have illuminated individual steps in the reaction cycle of the Escherichia coli Hsp70 molecular chaperone DnaK. Using this new information, we compare two distinctly different global mechanisms of action--holding versus unfolding--and argue that the available evidence suggests that DnaK is an unfoldase.
Publication types
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Comparative Study
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Adenosine Triphosphate / metabolism
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Computer Simulation
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Escherichia coli Proteins / chemistry
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Escherichia coli Proteins / genetics
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Escherichia coli Proteins / metabolism*
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HSP70 Heat-Shock Proteins / chemistry
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HSP70 Heat-Shock Proteins / metabolism*
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Models, Biological
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Models, Molecular
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Molecular Chaperones / chemistry
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Molecular Chaperones / metabolism*
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Protein Biosynthesis
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Protein Folding
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Protein Processing, Post-Translational
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Protein Structure, Tertiary
Substances
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Escherichia coli Proteins
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HSP70 Heat-Shock Proteins
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Molecular Chaperones
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Adenosine Triphosphate
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dnaK protein, E coli