The functional interaction between HMGA1 and the estrogen receptor requires either the N- or the C-terminal domain of the receptor

FEBS Lett. 2004 Feb 13;559(1-3):89-95. doi: 10.1016/S0014-5793(04)00032-8.

Abstract

We have previously shown that HMGA1 enhances the transcriptional activity of promoters containing the estrogen response element (ERE) and increases binding of the estrogen receptor (ER) to ERE. Herein, we have assessed the transcriptional activity and ERE-binding ability of deleted ER fragments in absence or in presence of HMGA1. The HMGA1 protein stimulated binding and transcriptional activity by a factor of about 2-fold compared to the wild-type ER and both the N- and C-terminal ER deleted domains, but had no effect when both domains were deleted. These data show that HMGA1 cooperates with either the N- or the C-terminal transcriptional activation domain of the ER.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Line
  • Estrogen Receptor alpha
  • HMGA1a Protein / genetics
  • HMGA1a Protein / metabolism*
  • HMGA1a Protein / physiology
  • Humans
  • Peptide Fragments / metabolism
  • Protein Binding
  • Protein Structure, Tertiary
  • Receptors, Estrogen / chemistry*
  • Receptors, Estrogen / genetics
  • Receptors, Estrogen / metabolism*
  • Response Elements
  • Sequence Deletion
  • Transcription, Genetic
  • Transcriptional Activation
  • Transfection

Substances

  • Estrogen Receptor alpha
  • Peptide Fragments
  • Receptors, Estrogen
  • HMGA1a Protein