Fellinger, Karin and Rothbauer, Ulrich and Felle, Max and Laengst, Gernot and Leonhardt, Heinrich (2009) Dimerization of DNA Methyltransferase 1 Is Mediated by Its Regulatory Domain. JOURNAL OF CELLULAR BIOCHEMISTRY, 106 (4). pp. 521-528. ISSN 0730-2312, 1097-4644
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DNA methylation is a major epigenetic modification and plays a crucial role in the regulation of gene expression. Within the family of DNA methyltransferases (Dnmts), Dnmt3a and 3b establish methylation marks during early development, while Dnmt 1 maintains methylation patterns after DNA replication. The maintenance function of Dnmt 1 is regulated by its large regulatory N-terminal domain that interacts with other chromatin factors and is essential for the recognition of hemi-methylated DNA. Gelfiltration analysis showed that purified Dnmt 1 elutes at an apparent molecular weight corresponding to the size of a dimer. With protein interaction assays We could show that Dnmt 1 interacts with itself through its N-terminal regulatory domain. By deletion analysis and co-immunoprecipitations we mapped the dimerization domain to the targeting sequence TS that is located in the center of the N-terminal domain (amino acids 310-629) and was previously shown to mediate replication independent association with heterochromatin at chromocenters. Further mutational analyses suggested that the dimeric complex has a bipartite interaction interface and is formed in a head-to-head orientation. Dnmt 1 dimer formation could facilitate the discrimination of hemi-methylated target sites as has been found for other palindromic DNA sequence recognizing enzymes. These results assign an additional function to the TS domain and raise the interesting question how these functions are spatially and temporarily co-ordinated. J. Cell. Biochem. 106: 521-528, 2009. (C) 2009 Wiley-Liss, Inc.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | DE-NOVO; PROTEIN INTERACTIONS; MAINTENANCE METHYLATION; FLUORESCENT PROTEINS; CATALYTIC DOMAIN; LIVING CELLS; DNMT1; REPLICATION; GENE; EXPRESSION; DIMER; METHYLATION; DNA METHYLTRANSFERASE 1; Dnmt 1; TARGETING SEQUENCE |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Biochemie III > Prof. Dr. Gernot Längst |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 22 Sep 2020 11:03 |
| Last Modified: | 22 Sep 2020 11:03 |
| URI: | https://pred.uni-regensburg.de/id/eprint/29383 |
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