CHIP interacts with heat shock factor 1 during heat stress.
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.
Kim
Soo-A
SA
Oral Biology Research Institute, Chosun University College of Dentistry, 375 Seosuk-dong, Dong-gu, Gwangju 501-759, Republic of Korea.
Yoon
Jung-Hoon
JH
Kim
Do-Kyung
DK
Kim
Su-Gwan
SG
Ahn
Sang-Gun
SG
D001665:Binding Sites; D002942:Circular Dichroism; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D000076249:Heat Shock Transcription Factors; D006358:Hot Temperature; D006801:Humans; D011485:Protein Binding; D011487:Protein Conformation; D013312:Stress, Physiological; D014157:Transcription Factors / Q000737:chemistry / Q000378:metabolism*; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism*
D004268:DNA-Binding Proteins; C000619706:HSF1 protein, human; D000076249:Heat Shock Transcription Factors; D014157:Transcription Factors; C467728:STUB1 protein, human; D044767:Ubiquitin-Protein Ligases