Specific interaction of the 70-kDa heat shock cognate protein with the tetratricopeptide repeats.
Using a yeast two-hybrid system with the 70-kDa heat shock cognate protein (hsc70) or its C-terminal 30-kDa domain as baits, we isolated several proteins interacting with hsc70, including Hip/p48 and p60/Hop. Both are known to interact with hsc70. Except for Hip/p48, all of the proteins that we isolated interact with ... the 30-kDa domain. Moreover, the EEVD motif at the C terminus of the 30-kDa domain appears essential for this interaction. Sequence analysis of these hsc70-interacting proteins reveals that they all contain tetratricopeptide repeats. Using deletion mutants of these proteins, we demonstrated either by two-hybrid or in vitro binding assays that the tetratricopeptide repeat domains in these proteins are necessary and sufficient for mediating the interaction with hsc70.
Mesh Terms:
Amino Acid Sequence, Animals, Antigens, Neoplasm, Binding Sites, Carrier Proteins, Glutathione Transferase, HSC70 Heat-Shock Proteins, HSP70 Heat-Shock Proteins, Humans, Molecular Chaperones, Molecular Sequence Data, Mutation, Protein Binding, Protein Structure, Tertiary, Proteins, Rats, Recombinant Fusion Proteins, Repetitive Sequences, Amino Acid, Two-Hybrid System Techniques
Amino Acid Sequence, Animals, Antigens, Neoplasm, Binding Sites, Carrier Proteins, Glutathione Transferase, HSC70 Heat-Shock Proteins, HSP70 Heat-Shock Proteins, Humans, Molecular Chaperones, Molecular Sequence Data, Mutation, Protein Binding, Protein Structure, Tertiary, Proteins, Rats, Recombinant Fusion Proteins, Repetitive Sequences, Amino Acid, Two-Hybrid System Techniques
J. Biol. Chem.
Date: Nov. 26, 1999
PubMed ID: 10567422
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