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Characterization of native interaction of hsp110 with hsp25 and hsc70
Author(s) -
Wang Xiang-Yang,
Chen Xing,
Oh Hyun-Ju,
Repasky Elizabeth,
Kazim Latif,
Subjeck John
Publication year - 2000
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/s0014-5793(99)01733-0
Subject(s) - immunoprecipitation , chaperone (clinical) , heat shock protein , hsp70 , biology , in vitro , microbiology and biotechnology , mutant , peptide , biochemistry , cell culture , genetics , gene , medicine , pathology
The 110 kDa heat shock protein (HSP) (hsp110) has been shown to be a diverged subgroup of the hsp70 family and is one of the major HSPs in mammalian cells [1,2]. In examining the native interactions of hsp110, we observed that it is found to reside in a large molecular complex. Immunoblot analysis and co‐immunoprecipitation studies identified two other HSPs as components of this complex, hsc70 and hsp25. When examined in vitro, purified hsp25, hsp70 and hsp110 were observed to spontaneously form a large complex and to directly interact with one another. When luciferase was added to this in vitro system, it was observed to migrate into this chaperone complex following heat shock. Examination of two deletion mutants of hsp110 demonstrated that its peptide‐binding domain is required for interaction with hsp25, but not with hsc70. The potential function of the hsp110‐hsc70‐hsp25 complex is discussed.