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Oligomerization and binding of the Dnmt3a DNA methyltransferase to parallel DNA molecules

Jurkowska, Renata Z. ORCID:, Rajavelu, Arumugam, Anspach, Nils, Urbanke, Claus, Jankevicius, Gytis, Ragozin, Sergey, Nellen, Wolfgang and Jeltsch, Albert 2011. Oligomerization and binding of the Dnmt3a DNA methyltransferase to parallel DNA molecules. Journal of Biological Chemistry 286 (27) , pp. 24200-24207. 10.1074/jbc.M111.254987

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Structural studies showed that Dnmt3a has two interfaces for protein-protein interaction in the heterotetrameric Dnmt3a/3L C-terminal domain complex: the RD interface (mediating the Dnmt3a-3a contact) and the FF interface (mediating the Dnmt3a-3L contact). Here, we demonstrate that Dnmt3a-C forms dimers via the FF interface as well, which further oligomerize via their RD interfaces. Each RD interface of the Dnmt3a-C oligomer creates an independent DNA binding site, which allows for binding of separate DNA molecules oriented in parallel. Because Dnmt3L does not have an RD interface, it prevents Dnmt3a oligomerization and binding of more than one DNA molecule. Both interfaces of Dnmt3a are necessary for the heterochromatic localization of the enzyme in cells. Overexpression of Dnmt3L in cells leads to the release of Dnmt3a from heterochromatic regions, which may increase its activity for methylation of euchromatic targets like the differentially methylated regions involved in imprinting.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Publisher: American Society for Biochemistry and Molecular Biology
ISSN: 0021-9258
Date of First Compliant Deposit: 30 March 2021
Last Modified: 04 May 2023 20:23

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