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Isolation and characterization of a DnaJ-like protein in rats: the C-terminal 10-kDa domain of hsc70 is not essential for stimulating the ATP-hydrolytic activity of hsc70 by a DnaJ-like protein.

Authors: Leng, CH  Brodsky, JL  Wang, C 
Citation: Leng CH, etal., Protein Sci 1998 May;7(5):1186-94.
Pubmed: (View Article at PubMed) PMID:9605323
DOI: Full-text: DOI:10.1002/pro.5560070513

A DnaJ-like protein, RDJ1, was isolated from a rat brain cDNA library. The protein is predicted to have 397 amino acid residues and shares 99% identity to that of HDJ2, a human DnaJ-like protein. RDJ1 was also shown to rescue the temperature-sensitive lethality of a strain containing a mutated cytosolic DnaJ in yeast, ydj1-151. Fragments containing the J-domain of RDJ1 either with or without the G/F motif were expressed in Escherichia coli. The purified proteins stimulated the ATPase activity of hsc70 and of the 60-kDa N-terminal fragment of hsc70. These results imply that RDJ1 can interact with the N-terminal 60-kDa fragment of hsc70 to activate ATP hydrolysis by hsc70.


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RGD Object Information
RGD ID: 633115
Created: 2003-08-29
Species: All species
Last Modified: 2003-08-29
Status: ACTIVE


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