Modifying chromatin to permit steroid hormone receptor-dependent transcription

• Published in: BBA - Gene Structure and Expression 2004-03, Vol.1677 (1), p.30-45
• Main Authors: Kinyamu, H.Karimi, Archer, Trevor K.
• Format: Article
• Language: English
• Subjects: Adenosine Triphosphate - metabolism; Animals; Cell Nucleus - genetics; Cell Nucleus - metabolism; Chromatin; Chromatin Assembly and Disassembly; Chromatin remodeling; Cysteine Endopeptidases - metabolism; Histone Deacetylases - metabolism; Histone modification; Histones - metabolism; Humans; Macromolecular Substances; Methylation; Multienzyme Complexes - metabolism; Phosphorylation; Proteasome; Proteasome Endopeptidase Complex; Receptors, Steroid - genetics; Receptors, Steroid - metabolism; Steroid hormone receptor; Transcription; Transcription, Genetic; Ubiquitin - metabolism
• ISSN: 0167-4781; 0006-3002; 1879-2634
• DOI: 10.1016/j.bbaexp.2003.09.015

Lipophilic hormones, including steroids, exert their physiological effects through binding to high-affinity superfamily of steroid hormone receptor (SR) proteins that function as ligand-dependent DNA binding transcription factors. To date, SR proteins are among a few transcription factors shown to directly interact with higher order chromatin structures to regulate gene expression. To perturb chromatin, SRs employ enzymatic multicomplexes that can either remodel or modify chromatin. Here we examine the current state of knowledge concerning multicomplex chromatin remodeling/modification machines and SR-dependent transcription. We will focus on the role of these protein–protein and chromatin–protein interactions in vivo with the MMTV promoter as a primary model. In addition, we discuss emerging evidence implicating chaperone proteins and proteasome degradation machinery in SR-mediated gene regulation within chromatin.