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 journalArticle

15 Citations (Scopus)

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)2527-2537
Number of pages11
JournalEuropean Journal of Biochemistry
Volume269
Issue number10
DOIs
Publication statusPublished - 2002

Fingerprint

Heat-Shock Response
Consensus Sequence
Response Elements
Shock
SELEX Aptamer Technique
Hot Temperature
Embryonal Carcinoma Stem Cells
Tumors
Genes
Chemical activation
Cells
Ligands
DNA
Neoplasms
Proteins
heat shock transcription factor
In Vitro Techniques

Keywords

  • Consensus binding sequence
  • Cooperativity
  • Heat shock transcription factor-2
  • Protein purification
  • SELEX

ASJC Scopus subject areas

  • Biochemistry

Cite this

Determination of the consensus binding sequence for the purified embryonic heat shock factor 2. / Manuel, Martine; Rallu, Murielle; Loones, Marie Thérèse; Zimarino, Vincenzo; Mezger, Valérie; Morange, Michel.

In: European Journal of Biochemistry, Vol. 269, No. 10, 2002, p. 2527-2537.

Research output: Contribution to journalArticle

Manuel, Martine ; Rallu, Murielle ; Loones, Marie Thérèse ; Zimarino, Vincenzo ; Mezger, Valérie ; Morange, Michel. / Determination of the consensus binding sequence for the purified embryonic heat shock factor 2. In: European Journal of Biochemistry. 2002 ; Vol. 269, No. 10. pp. 2527-2537.
@article{225f88bb253e4d6c9c7affd1d2296248,
title = "Determination of the consensus binding sequence for the purified embryonic heat shock factor 2",
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.",
keywords = "Consensus binding sequence, Cooperativity, Heat shock transcription factor-2, Protein purification, SELEX",
author = "Martine Manuel and Murielle Rallu and Loones, {Marie Th{\'e}r{\`e}se} and Vincenzo Zimarino and Val{\'e}rie Mezger and Michel Morange",
year = "2002",
doi = "10.1046/j.1432-1033.2002.02917.x",
language = "English",
volume = "269",
pages = "2527--2537",
journal = "European Journal of Biochemistry",
issn = "0014-2956",
publisher = "Wiley-Blackwell",
number = "10",

}

TY - JOUR

T1 - Determination of the consensus binding sequence for the purified embryonic heat shock factor 2

AU - Manuel, Martine

AU - Rallu, Murielle

AU - Loones, Marie Thérèse

AU - Zimarino, Vincenzo

AU - Mezger, Valérie

AU - Morange, Michel

PY - 2002

Y1 - 2002

N2 - 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.

AB - 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.

KW - Consensus binding sequence

KW - Cooperativity

KW - Heat shock transcription factor-2

KW - Protein purification

KW - SELEX

UR - http://www.scopus.com/inward/record.url?scp=0036106790&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036106790&partnerID=8YFLogxK

U2 - 10.1046/j.1432-1033.2002.02917.x

DO - 10.1046/j.1432-1033.2002.02917.x

M3 - Article

VL - 269

SP - 2527

EP - 2537

JO - European Journal of Biochemistry

JF - European Journal of Biochemistry

SN - 0014-2956

IS - 10

ER -