NDLI: Cooperative DNA binding and protein/DNA fiber formation increases the activity of the Dnmt3a DNA methyltransferase.

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Cooperative DNA binding and protein/DNA fiber formation increases the activity of the Dnmt3a DNA methyltransferase.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Jeltsch, Albert Reinhardt, Richard Jurkowska, Renata Z. Rajavelu, Arumugam Emperle, Max
Description	Author Affiliation: Emperle M ( From the Institute of Biochemistry, Stuttgart University, D-70569 Stuttgart, Germany and.); Rajavelu A ( From the Institute of Biochemistry, Stuttgart University, D-70569 Stuttgart, Germany and.); Reinhardt R ( Max-Planck-Genomzentrum Köln, D-50829 Köln, Germany.); Jurkowska RZ ( From the Institute of Biochemistry, Stuttgart University, D-70569 Stuttgart, Germany and renata.jurkowska@ibc.uni-stuttgart.de.); Jeltsch A ( From the Institute of Biochemistry, Stuttgart University, D-70569 Stuttgart, Germany and albert.jeltsch@ibc.uni-stuttgart.de.)
Abstract	The Dnmt3a DNA methyltransferase has been shown to bind cooperatively to DNA and to form large multimeric protein/DNA fibers. However, it has also been reported to methylate DNA in a processive manner, a property that is incompatible with protein/DNA fiber formation. We show here that the DNA methylation rate of Dnmt3a increases more than linearly with increasing enzyme concentration on a long DNA substrate, but not on a short 30-mer oligonucleotide substrate. We also show that addition of a catalytically inactive Dnmt3a mutant, which carries an amino acid exchange in the catalytic center, increases the DNA methylation rate by wild type Dnmt3a on the long substrate but not on the short one. In agreement with this finding, preincubation experiments indicate that stable protein/DNA fibers are formed on the long, but not on the short substrate. In addition, methylation experiments with substrates containing one or two CpG sites did not provide evidence for a processive mechanism over a wide range of enzyme concentrations. These data clearly indicate that Dnmt3a binds to DNA in a cooperative reaction and that the formation of stable protein/DNA fibers increases the DNA methylation rate. Fiber formation occurs at low µm concentrations of Dnmt3a, which are in the range of Dnmt3a concentrations in the nucleus of embryonic stem cells. Understanding the mechanism of Dnmt3a is of vital importance because Dnmt3a is a hotspot of somatic cancer mutations one of which has been implicated in changing Dnmt3a processivity.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	43
Volume Number	289
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2014-10-24
Publisher Place	United States
Access Restriction	Open
Subject Keyword	DNA (Cytosine-5-)-Methyltransferase Metabolism DNA Animals Biocatalysis Cell Nucleus DNA Methylation Embryonic Stem Cells Enzymology Fluorescence Kinetics Mice Molecular Sequence Data Mutant Proteins Nucleotide Motifs Genetics Protein Binding Protein Multimerization Sequence Analysis, DNA Substrate Specificity Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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