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Interaction between hsp70 and hsp40, eukaryotic homologues of DnaK and DnaJ, in human cells expressing mutant‐type p53
Author(s) -
Sugito Kazuhiro,
Yamane Mitsuo,
Hattori Hirotomo,
Hayashi Yasushi,
Tohnai Iwai,
Ueda Minoru,
Tsuchida Nobuo,
Ohtsuka Kenzo
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01417-y
Subject(s) - immunoprecipitation , chaperone (clinical) , mutant , hsp70 , biology , heat shock protein , suppressor , microbiology and biotechnology , gene , biochemistry , medicine , pathology
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 α‐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.