Regulation of Hsp70 function by a eukaryotic DnaJ homolog.

@article{Cyr1992RegulationOH,
  title={Regulation of Hsp70 function by a eukaryotic DnaJ homolog.},
  author={Douglas M. Cyr and Xu Lu and Michael G. Douglas},
  journal={The Journal of biological chemistry},
  year={1992},
  volume={267 29},
  pages={20927-31}
}
We report that a purified cytoplasmic Hsp70 homolog from Saccharomyces cerevisiae, Hsp70SSA1, exhibits a weak ATPase activity, which is stimulated by a purified eukaryotic dnaJp homolog (YDJ1p). Stable complex formation between Hsp70SSA1 and the permanently unfolded protein carboxymethylated alpha-lactalbumin (CMLA) was assayed by native gel electrophoresis. The affinity of Hsp70SSA1 for CMLA appeared to be regulated by YDJ1p. Significant reduction in both CMLA-Hsp70SSA1 complex formation and… CONTINUE READING

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