Abstract
K+ is an indispensable cofactor for ATPase activity of eukaryotic cytosolic Hsp70 chaperone systems which lack a GrpE homolog. In the case of the bacterial Hsp70 (DnaK) system, GrpE, a nucleotide exchange factor, stimulates ATPase activity but little is known about the effect of K+. Here, we have cloned a grpE gene from a thermophile, Thermus thermophilus, and purified a homodimeric GrpE protein. Using proteins of this bacterium, we found that the GrpE stimulation of ATPase activity of DnaK x DnaJ complex was absolutely dependent on the presence of K+.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphatases / metabolism*
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Amino Acid Sequence
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics
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Bacterial Proteins / physiology*
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Cloning, Molecular
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Dimerization
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Drug Synergism
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Escherichia coli Proteins*
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HSP40 Heat-Shock Proteins
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HSP70 Heat-Shock Proteins / drug effects
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HSP70 Heat-Shock Proteins / metabolism*
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Heat-Shock Proteins / chemistry
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Heat-Shock Proteins / drug effects
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Heat-Shock Proteins / genetics
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Heat-Shock Proteins / metabolism*
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Heat-Shock Proteins / physiology*
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Molecular Sequence Data
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Potassium / physiology*
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Thermus thermophilus / enzymology*
Substances
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Bacterial Proteins
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DnaJ protein, E coli
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Escherichia coli Proteins
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GrpE protein, Bacteria
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HSP40 Heat-Shock Proteins
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HSP70 Heat-Shock Proteins
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Heat-Shock Proteins
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Adenosine Triphosphatases
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dnaK protein, E coli
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Potassium