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Published online 17 May 2004

Nucleic Acids Research, 2004, Vol. 32, No. 9 2716-2729
© 2004 Oxford University Press

Isolation and characterization of a novel DNA methyltransferase complex linking DNMT3B with components of the mitotic chromosome condensation machinery

Theresa M. Geiman, Umesh T. Sankpal, Andrea K. Robertson, Yue Chen1, Manjari Mazumdar2, Jason T. Heale3, John A. Schmiesing3, Wankee Kim4, Kyoko Yokomori3, Yingming Zhao1 and Keith D. Robertson*

Epigenetic Gene Regulation and Cancer Section and 2 Cell Biology and Gene Expression Section, LRBGE/NCI/NIH, Bethesda, MD 20892, USA, 1 Department of Biochemistry, UT Southwestern Medical Center, Dallas, TX 75390, USA, 3 Department of Biological Chemistry, University of California, Irvine, CA 92697, USA and 4 Institute for Medical Sciences, School of Medicine, Ajou University, Suwon, South Korea

*To whom correspondence should be addressed at present address: University of Florida, Department of Biochemistry and Molecular Biology, Box 100245, Gainesville, FL 32610, USA. Tel: +1 301 594 9509; Fax: +1 301 496 4951; Email: keithr{at}ufl.edu

Received January 8, 2004; Revised March 26, 2004; Accepted April 15, 2004

Proper patterns of genome-wide DNA methylation, mediated by DNA methyltransferases DNMT1, -3A and -3B, are essential for embryonic development and genomic stability in mammalian cells. The de novo DNA methyltransferase DNMT3B is of particular interest because it is frequently overexpressed in tumor cells and is mutated in immunodeficiency, centromere instability and facial anomalies (ICF) syndrome. In order to gain a better understanding of DNMT3B, in terms of the targeting of its methylation activity and its role in genome stability, we biochemically purified endogenous DNMT3B from HeLa cells. DNMT3B co-purifies and interacts, both in vivo and in vitro, with several components of the condensin complex (hCAP-C, hCAP-E and hCAP-G) and KIF4A. Condensin mediates genome-wide chromosome condensation at the onset of mitosis and is critical for proper segregation of sister chromatids. KIF4A is proposed to be a motor protein carrying DNA as cargo. DNMT3B also interacts with histone deacetylase 1 (HDAC1), the co-repressor SIN3A and the ATP-dependent chromatin remodeling enzyme hSNF2H. Further more, DNMT3B co-localizes with condensin and KIF4A on condensed chromosomes throughout mitosis. These studies therefore reveal the first direct link between the machineries regulating DNA methylation and mitotic chromosome condensation in mammalian cells.


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