CHIP interacts with heat shock factor 1 during heat stress

FEBS Lett. 2005 Dec 5;579(29):6559-63. doi: 10.1016/j.febslet.2005.10.043. Epub 2005 Nov 2.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Circular Dichroism
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / metabolism*
  • Heat Shock Transcription Factors
  • Hot Temperature*
  • Humans
  • Protein Binding
  • Protein Conformation
  • Stress, Physiological*
  • Transcription Factors / chemistry
  • Transcription Factors / metabolism*
  • Ubiquitin-Protein Ligases / metabolism*

Substances

  • DNA-Binding Proteins
  • HSF1 protein, human
  • Heat Shock Transcription Factors
  • Transcription Factors
  • STUB1 protein, human
  • Ubiquitin-Protein Ligases