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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
Author(s) -
Leng ChihHsiang,
Wang Chung,
Brodsky Jeffrey L.
Publication year - 1998
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560070513
Subject(s) - biology , escherichia coli , biochemistry , complementary dna , cytosol , atp hydrolysis , inhibitor protein , microbiology and biotechnology , atpase , recombinant dna , enzyme , gene
Abstract 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 RDJl 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 RDJl can interact with the N‐terminal 60‐kDa fragment of hsc70 to activate ATP hydrolysis by hsc70.