Function of steroidogenic factor 1 (SF1) ligand-binding domain in gene activation and interaction with AP1

Lih Ann Li, Deepak Lala, Bon Chu Chung

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

The nuclear receptor SF1 is an essential mediator in ventromedial hypothalamus-pituitary-gonadal development. As with other nuclear receptors, SF1 possesses a DNA-binding domain composed of two zinc fingers and a ligand-binding domain containing a ligand-dependent activation sequence termed AF2. To dissect the domain function of SF1, we examined various SF1 mutants in mouse adrenocortical Y1 cells and human placental JEG3 cells. Destruction of the AF2 structure removed 73-90% transactivation activity, suggesting that AF2 is indispensable for transactivation. Mutants carrying the DNA-binding domain but lacking the AF2 or the ligand-binding domain blocked the activity of normal SF1. Disrupting the zinc finger diminished the dominant negative effect of mutant. Cotransfection of SF1 with AP1 showed that the two transcription factors cooperated to activate gene expression. Some mutants lost the synergistic action with AP1, while some retained partial activity. These experiments delineate the functional domains of SF1.

Original languageEnglish
Pages (from-to)318-320
Number of pages3
JournalBiochemical and Biophysical Research Communications
Volume250
Issue number2
DOIs
Publication statusPublished - Sep 18 1998

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Function of steroidogenic factor 1 (SF1) ligand-binding domain in gene activation and interaction with AP1'. Together they form a unique fingerprint.

  • Cite this