Molecular Mechanism of Action of Plant DRM De Novo DNA Methyltransferases

• Published in: Cell Vol. 157; no. 5; pp. 1050 - 1060
• Main Authors: Zhong, Xuehua, Du, Jiamu, Hale, Christopher J., Gallego-Bartolome, Javier, Feng, Suhua, Vashisht, Ajay A., Chory, Joanne, Wohlschlegel, James A., Patel, Dinshaw J., Jacobsen, Steven E.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 22.05.2014
• Subjects: Amino Acid Sequence; Arabidopsis; Arabidopsis - enzymology; Arabidopsis - metabolism; Arabidopsis Proteins - metabolism; Argonaute Proteins - metabolism; catalytic activity; Catalytic Domain; correlation; crystal structure; DNA; DNA methylation; DNA-directed RNA polymerase; epigenetics; loci; mechanism of action; messenger RNA; methyltransferases; Methyltransferases - chemistry; Methyltransferases - metabolism; Models, Molecular; Molecular Sequence Data; Nicotiana - enzymology; Nicotiana - metabolism; non-coding RNA; small interfering RNA; tobacco

DNA methylation is a conserved epigenetic gene-regulation mechanism. DOMAINS REARRANGED METHYLTRANSFERASE (DRM) is a key de novo methyltransferase in plants, but how DRM acts mechanistically is poorly understood. Here, we report the crystal structure of the methyltransferase domain of tobacco DRM (N...