ArticleProtein science : a publication of the Protein Society1998
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.
Article in Protein science : a publication of the Protein Society, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 9 citations in OpenAlex.
- Expression of a malarial Hsp70 improves defects in chaperone-dependent activities in ssa1 mutant yeast.PloS one · 2011Article
- Cloning and molecular characterization of heat shock cognate 70 from tiger shrimp (Penaeus monodon).Cell stress & chaperones · 2004Article
- Divergent functional properties of the ribosome-associated molecular chaperone Ssb compared with other Hsp70s.Molecular biology of the cell · 2001Article
- Different combinations of the heat-shock cognate protein 70 (hsc70) C-terminal functional groups are utilized to interact with distinct tetratricopeptide repeat-containing proteins.The Biochemical journal · 2001Article
- Interaction of murine BiP/GRP78 with the DnaJ homologue MTJ1.The Journal of biological chemistry · 2000Article
- Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for their classification and nomenclature.Cell stress & chaperones · 2000Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
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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 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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Registered trials
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