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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Interaction between hsp70 and hsp40, eukaryotic homologues of DnaK and DnaJ, in human cells expressing mutant-type p53.

We have recently identified a novel 40-kDa heatshock protein hsp40 as a mammalian homologue of bacterial DnaJ protein. Here we demonstrate the physical interaction between hsp70 (DnaK homologue) and hsp40 in human cells as determined by immunoprecipitation methods. Co-immunoprecipitation of hsp70 with hsp40 was dependent on the presence of ATP or unfolded protein (reduced carboxymethylated alpha-lactalbumin). A mutant type of tumor suppressor gene product, mtp53, was co-immunoprecipitated not only with hsp70 but also with hsp40. These results suggest the existence of a hsp70(DnaK)/hsp40(DnaJ) chaperone system in mammalian cells.[1]

References

  1. Interaction between hsp70 and hsp40, eukaryotic homologues of DnaK and DnaJ, in human cells expressing mutant-type p53. Sugito, K., Yamane, M., Hattori, H., Hayashi, Y., Tohnai, I., Ueda, M., Tsuchida, N., Ohtsuka, K. FEBS Lett. (1995) [Pubmed]
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