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Molecular and Cellular Biology, May 2003, p. 3226-3236, Vol. 23, No. 9
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.9.3226-3236.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

The Methyl-CpG Binding Protein MBD1 Interacts with the p150 Subunit of Chromatin Assembly Factor 1

Brian E. Reese,1,2 Kurtis E. Bachman,1,{dagger} Stephen B. Baylin,1* and Michael R. Rountree1,{ddagger}

Tumor Biology Division, The Sidney Kimmel Comprehensive Cancer Center,1 Graduate Program in Cellular and Molecular Medicine, The Johns Hopkins University School of Medicine, Baltimore, Maryland2

Received 29 July 2002/ Returned for modification 17 September 2002/ Accepted 4 February 2003

DNA promoter hypermethylation has been shown to be a functional mechanism of transcriptional repression. This epigenetic gene silencing is thought to involve the recruitment of chromatin-remodeling factors, such as histone deacetylases, to methylated DNA via a family of proteins called methyl-CpG binding proteins (MBD1 to -4). MBD1, a member of this family, exhibits transcription-repressive activity, but to this point no interacting protein partners have been identified. In this study, we demonstrate that MBD1 partners with the p150 subunit of chromatin assembly factor 1 (CAF-1), forming a multiprotein complex that also contains HP1{alpha}. The MBD1-CAF-1 p150 interaction requires the methyl-CpG binding domain of MBD1, and the association occurs in the C terminus of CAF-1 p150. The two proteins colocalize to regions of dense heterochromatin in mouse cells, and overexpression of the C terminus of CAF-1 p150 prevents the targeting of MBD1 in these cells without disrupting global heterochromatin structure. This interaction suggests a role for MBD1 and CAF-1 p150 in methylation-mediated transcriptional repression and the inheritance of epigenetically determined chromatin states.

* Corresponding author. Present address: Cancer Research Building, Room 541, 1650 Orleans St., Baltimore, MD 21231. Phone: (410) 955-8506. Fax: (410) 614-9884. E-mail: sbaylin{at}jhmi.edu.

{dagger} Present address: The Howard Hughes Medical Institute, The Johns Hopkins University School of Medicine, Baltimore, MD 21231.

{ddagger} Present address: Department of Molecular Pharmacology, St. Jude Children's Research Hospital, Memphis, TN 38105.

Molecular and Cellular Biology, May 2003, p. 3226-3236, Vol. 23, No. 9
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.9.3226-3236.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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