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Estrogen receptor accessory proteins: effects on receptor-DNA interactions
C C Landel1, P J Kushner, G L Greene
1Department of Biochemistry and Molecular Biology, University of Chicago, IL 60637, USA.
Environmental Health Perspectives
|October 1, 1995
Summary
Accessory proteins, including heat shock protein 70 (hsp70) and protein disulfide isomerase (PDI), are crucial for optimal estrogen receptor (ER) interaction with estrogen response elements (EREs). These proteins enhance ER-DNA binding stability, highlighting their role in ER function.
Area of Science:
- Molecular Biology
- Cellular Biology
- Endocrinology
Background:
- Steroid receptors, like the estrogen receptor (ER), have well-defined structures, but the function of associated proteins remains largely unknown.
- Understanding these accessory proteins is key to elucidating the full mechanism of ER activity.
Purpose of the Study:
- To identify and characterize proteins that associate with the human estrogen receptor (hER).
- To investigate the role of these associated proteins in mediating hER function, particularly its interaction with DNA.
Main Methods:
- Immunoaffinity chromatography
- Steroid affinity chromatography
- Site-specific DNA-affinity chromatography
- Protein identification using established biochemical techniques
Main Results:
- Identified heat shock protein 70 (hsp70) and protein disulfide isomerase (PDI) as associated with hER.
- Discovered two unidentified proteins (p48, p45) that preferentially bind to ER-specific DNA elements.
- Demonstrated that the presence of these four accessory proteins significantly enhances the stability of the hER-estrogen response element (ERE) complex by increasing the association rate.
Conclusions:
- Accessory proteins, including hsp70 and PDI, play a vital role in mediating estrogen receptor (ER) function.
- These proteins are essential for the optimal interaction of ER with estrogen response elements (EREs), suggesting a requirement for these factors in regulating ER-mediated gene transcription.