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CHIP interacts with heat shock factor 1 during heat stress
Author(s) -
Kim Soo-A,
Yoon Jung-Hoon,
Kim Do-Kyung,
Kim Su-Gwan,
Ahn Sang-Gun
Publication year - 2005
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/j.febslet.2005.10.043
Subject(s) - hsf1 , heat shock factor , transactivation , heat shock protein , heat shock , shock (circulatory) , chip , biophysics , chemistry , microbiology and biotechnology , hsp70 , biology , gene , transcription factor , biochemistry , medicine , computer science , telecommunications
Heat shock factor 1 (HSF1) is a major transactivator of heat shock genes in response to stress and mediates cell protection against various harmful conditions. In this study, we identified the interaction of CHIP (carboxyl terminus of the heat shock cognate protein 70‐interacting protein) with the N‐terminus of HSF1. Using GST full‐down assay, we found that CHIP directly interacts with C‐terminal deleted HSF1 (a.a. 1–290) but not with full‐length HSF1 under non‐stressed conditions. Interestingly, interaction of CHIP with full‐length HSF1 was induced by heat shock treatment. The structural change of HSF1 was observed under heat stressed conditions by CD spectra. These observations demonstrate the direct interaction between HSF1 and CHIP and this interaction requires conformational change of HSF1 by heat stress.