Exp Mol Med.
2007 Aug;39(4):544-555.
The functional role of the CARM1-SNF5 complex and its associated HMT activity in transcriptional activation by thyroid hormone receptor
- Affiliations
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- 1Department of Biochemistry and Molecular Biology, Center for Chronic Metabolic Disease Research, Yonsei University College of Medicine Seoul 120-752, Korea. yhgeun@yumc.yonsei.ac.kr, kimkh34@yumc.yonsei.ac.kr
- 2Brain Korea 21 Project for Medical Sciences, Yonsei University College of Medicine, Seoul 120-752, Korea.
- 3Howard Hughes Medical Institute, Program in Gene Function and Expression, University of Massachusetts Medical School, Worcester, MA 01605, USA.
- 4Department of Chemical Engineering, College of Engineering, Yonsei University, Seoul 120-749, Korea.
Abstract
- We have investigated the function and mechanisms of the CARM1-SNF5 complex in T3-dependent transcriptional activation. Using specific small interfering RNAs (siRNA) to knock down coactivators in HeLa alpha2 cells, we found that coactivator associated arginine methyltransferase 1 (CARM1) and SWI/SNF complex component 5 (SNF5) are important for T3-dependent transcriptional activation. The CARM1- SWI/SNF chromatin remodeling complex serves as a mechanism for the rapid reversal of H3-K9 methylation. Importantly, siRNA treatment against CARM1 and/or SNF5 increased the recruitment of HMTase G9a to the type 1 deiodinase (D1) promoter even with T3. Knocking- down either CARM1 or SNF5 also inhibited the down- regulation of histone macroH2A, which is correlated with transcriptional activation. Finally, knocking down CARM1 and SNF5 by siRNA impaired the association of these coactivators to the D1 promoter, suggesting functional importance of CARM1- SNF5 complex in T3-dependent transcriptional activation.
Keyword
MeSH Terms
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Chromosomal Proteins, Non-Histone/*physiology
DNA-Binding Proteins/*physiology
Hela Cells
Histone-Lysine N-Methyltransferase/*metabolism
Histones/metabolism
Humans
Iodide Peroxidase/metabolism
Methylation
Promoter Regions, Genetic
Protein Methyltransferases
Protein-Arginine N-Methyltransferase/*physiology
Receptors, Thyroid Hormone/*physiology
Transcription Factors/*physiology
*Transcriptional Activation
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