Determination of the consensus binding sequence for the purified embryonic heat shock factor 2

Martine Manuel, Murielle Rallu, Marie-Thérèse Loones, Vincenzo Zimarino, Valérie Mezger, Michel Morange

Research output: Contribution to journalArticlepeer-review

Abstract

Heat shock transcription factors (HSFs) are characterized by their ability, upon activation, to bind to heat shock response elements (HSE) present in the promoter of their target genes. HSE are composed of inverted repeats of the pentamer nGAAm. In this study, we compare the embryonic HSF2 protein, purified from F9 embryonal carcinoma cells tumor, and the in vitro synthesized HSF2. We show that the context of HSF2 synthesis influences its thermosensitivity and DNA-binding properties. Therefore, we determined the consensus binding sequence for the purified embryonic HSF2 by the technique of systematic evolution of ligands by exponential enrichment (SELEX). We show that embryonic HSF2 prefers sites containing three or four nGAAm inverted pentamers and that its optimal binding sequence contains the 8-mer palindromic core 5'-TTCTAGAA-3'. The consensus binding sequence for the embryonic HSF2 will be very helpful to identify new targets for this factor, during developmental and differentiation processes.

Original languageEnglish
Pages (from-to)2527-37
Number of pages11
JournalEuropean Journal of Biochemistry
Volume269
Issue number10
Publication statusPublished - May 2002

Keywords

  • Animals
  • Binding Sites
  • Cloning, Molecular
  • Consensus Sequence
  • DNA
  • Gene Library
  • Heat-Shock Proteins
  • Hot Temperature
  • Mice
  • Protein Binding
  • Transcription Factors
  • Tumor Cells, Cultured

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