No abstract

A cytosine-specific DNA methyltransferase (EC 2.1.1.37) has been purified to near homogeneity from a mealybug (Planococcus lilacinus). The enzyme can methylate cytosine residues in CpG sequences as well as CpA sequences. The apparent molecular weight of the enzyme was estimated as 135,000 daltons by FPLC. The enzyme exhibits a processive mode of action and a salt dependence similar to mammalian methylases. Mealybug methylase exhibits a preference for denatured DNA substrates.

No abstract

The levels of de novo DNA methyltransferase were studied during the development of a mealybug, PIanococcus lilacinus. No enzyme activity could be detected in extracts from second instar females. But the enzyme occurs at high levels in third instar females and is maintained at that level during fourth instar when gametogenesis, fertilization and chromosome imprinting occur. These results suggest a developmental stage-specific modulation of levels of DNA methyltransferase. Assays with synthetic polymers showed that the enzyme can methylate not only polymers containing GpG but also those containing CpA and CpI.