IMAGE: Image shows the DNMT3A-DNA complex. A research team led by Jikui Song cracked the crystal structure for DNMT3A-DNA complex. The structure reveals that DNMT3A molecules attack two substrate sites adjacent… view more
Credit: Song lab, UC Riverside.
RIVERSIDE, Calif. – A research team led by a biochemist at the University of California, Riverside has solved the crystal structure for an enzyme that plays a key role in DNA methylation, the process by which methyl groups are added to the DNA molecule.
DNA methylation alters gene expression. This fundamental cellular mechanism critically influences plant, animal, and human development. It is known to regulate genome stability and cell differentiation. In humans, errors in methylation have been associated with various diseases, including cancer.
In mammals, DNA methylation is established de novo (afresh) by closely related enzymes, DNMT3A and DNMT3B, during germ cell development and early embryonic development. One difficulty in understanding how de novo DNA methylation works is that the structures of these enzymes are not known.
The UC Riverside-led team has now solved the crystal structure for substrate-bound DNMT3A. This breakthrough reveals how the enzyme recognizes and methylates its substrates — important information for understanding de novo DNA methlylation. A
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