Eukaryotic DNA methylases and their use forin vitromethylation
- 30 January 1990
- journal article
- research article
- Published by The Royal Society in Philosophical Transactions of the Royal Society of London. B, Biological Sciences
- Vol. 326 (1235) , 189-198
- https://doi.org/10.1098/rstb.1990.0003
Abstract
DNA methylases from mouse and pea have been purified and characterized. Both are high molecular mass enzymes that show greater activity with hemimethylated than unmethylated substrate DNA. Both methylate cytosines in CpG preferentially, but not exclusively and show similar kinetics of methylation, which makes it difficult to saturate all possible sites on the DNA, but procedures are described that circumvent this problem.This publication has 33 references indexed in Scilit:
- Eukaryotic DNA methyltransferase: tissue and species distributionGene, 1988
- Structure of mouse DNA (cytosine-5-)-methyltransferaseEuropean Journal of Biochemistry, 1988
- Sp1 transcription factor binds DNA and activates transcription even when the binding site is CpG methylated.Genes & Development, 1988
- DNA methylation in wheatEuropean Journal of Biochemistry, 1987
- DNA methylation affects the formation of active chromatinCell, 1986
- Purification of human DNA (cytosine‐5‐)‐methyltransferaseJournal of Cellular Biochemistry, 1985
- Stimulation of de novo methylation following limited proteolysis of mouse ascites DNA methylaseFEBS Letters, 1983
- Characterization of DNA methyltransferase from bovine thymus cellsEuropean Journal of Biochemistry, 1983
- Program Evaluation and Program Development in Teacher Education: A Response to Katz et al. (1981)Journal of Teacher Education, 1981
- Deoxyribonucleic Acid Methyltransferase from the Eukaryote, Chlamydomonas reinhardiEuropean Journal of Biochemistry, 1980