Abstract
We investigated several hsp70/hsc70 interacting proteins and established by two independent techniques that hsp40 and Hop/p60 specifically interact with the 257 residue carboxy-terminal domain of hsp70 while Hap-46 and Hip/p48 bind the 383 residue amino-terminal ATP binding domain. Hap-46 and Hip/p48 competed for binding to hsc70, while Hap-46 had no effect on the binding of either Hop/p60 or hsp40 to hsc70. Hap-46 inhibited the refolding of thermally denatured firefly luciferase in an hsc70 and hsp40 dependent assay, and this effect was largely compensated by Hop/p60. These interacting proteins thus appear to cooperate in affecting the chaperoning activity of hsp70/hsc70.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Carrier Proteins / chemistry
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Carrier Proteins / metabolism*
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HSC70 Heat-Shock Proteins
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HSP40 Heat-Shock Proteins
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HSP70 Heat-Shock Proteins / chemistry
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HSP70 Heat-Shock Proteins / metabolism*
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Heat-Shock Proteins / chemistry
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Heat-Shock Proteins / metabolism
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Heating
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Humans
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Luciferases / metabolism
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Molecular Chaperones / chemistry
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Molecular Chaperones / metabolism*
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Protein Denaturation
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Protein Folding*
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Proteins / chemistry
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Proteins / metabolism*
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Recombinant Fusion Proteins / metabolism
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Tumor Suppressor Proteins*
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Yeasts / metabolism
Substances
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Carrier Proteins
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DNAJB1 protein, human
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HSC70 Heat-Shock Proteins
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HSP40 Heat-Shock Proteins
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HSP70 Heat-Shock Proteins
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HSPA8 protein, human
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Heat-Shock Proteins
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Molecular Chaperones
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Proteins
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Recombinant Fusion Proteins
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ST13 protein, human
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STIP1 protein, human
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Tumor Suppressor Proteins
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Luciferases