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Molecular and Cellular Biology, November 2003, p. 7475-7487, Vol. 23, No. 21
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.21.7475-7487.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

mSin3A/Histone Deacetylase 2- and PRMT5-Containing Brg1 Complex Is Involved in Transcriptional Repression of the Myc Target Gene cad

Sharmistha Pal,1 Romy Yun,1 Antara Datta,1 Lynne Lacomis,2 Hediye Erdjument-Bromage,2 Jitendra Kumar,1 Paul Tempst,2 and Saïd Sif1*

Department of Molecular and Cellular Biochemistry, College of Medicine and Public Health, The Ohio State University, Columbus, Ohio 43210,1 Molecular Biology Program, Memorial Sloan Kettering Cancer Center, New York, New York 100212

Received 17 July 2003/ Accepted 30 July 2003

The role of hSWI/SNF complexes in transcriptional activation is well characterized; however, little is known about their function in transcriptional repression. We have previously shown that subunits of the mSin3A/histone deacetylase 2 (HDAC2) corepressor complex copurify with hSWI/SNF complexes. Here we show that the type II arginine-specific methyltransferase PRMT5, which is involved in cyclin E repression, can be found in association with Brg1 and hBrm-based hSWI/SNF complexes. We also show that hSWI/SNF-associated PRMT5 can methylate hypoacetylated histones H3 and H4 more efficiently than hyperacetylated histones H3 and H4. Protein-protein interaction studies indicate that PRMT5 and mSin3A interact with the same hSWI/SNF subunits as those targeted by c-Myc. These observations prompted us to examine the expression profile of the c-Myc target genes, carbamoyl-phosphate synthase-aspartate carbamoyltransferase-dihydroorotase (cad) and nucleolin (nuc). We found that cad repression is altered in cells that express inactive Brg1 and in cells treated with the HDAC inhibitor depsipeptide. Using chromatin immunoprecipitation assays, we found that Brg1, mSin3A, HDAC2, and PRMT5 are directly recruited to the cad promoter. These results suggest that hSWI/SNF complexes, through their ability to interact with activator and repressor proteins, control expression of genes involved in cell growth and proliferation.

* Corresponding author. Mailing address: Department of Molecular and Cellular Biochemistry, Ohio State University College of Medicine, Columbus, OH 43210. Phone: (614) 247-7445. Fax: (614) 292-4118. E-mail: Sif.1{at}osu.edu.

Molecular and Cellular Biology, November 2003, p. 7475-7487, Vol. 23, No. 21
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.21.7475-7487.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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