Structure of mouse DNA (cytosine-5-)-methyltransferase.
DNA (cytosine-5-)-methyltransferase was purified as a single polypeptide (190 kDa by SDS-PAGE) from mouse P815 mastocytoma cells. This enzyme transfers methyl groups to unmethylated as well as to hemimethylated DNA sites with a strong preference for the hemimethylated substrate. A structural analysis of the isolated enzyme by electron microscopical techniques was undertaken. On the basis of the results obtained, we propose a model for the enzyme structure. This model describes the enzyme as a hemi-elliptical globular structure with dimensions of 5.4-6.7 nm for the height h and 10.3-10.8 nm for the diameter d, respectively; this globular structure bears a small appendix at the flat side. A molecular mass of 235-250 kDa is calculated from the measured dimensions. Limited trypsin digestion of the enzyme led to a 160-kDa fragment which preserved the gross morphology of the original material. The possible structure function relationships are discussed.
D000818:Animals; D004248:DNA (Cytosine-5-)-Methyltransferases / Q000032:analysis*; D005612:Freeze Drying; D012515:Mast-Cell Sarcoma / Q000201:enzymology; D051379:Mice; D008854:Microscopy, Electron; D008956:Models, Chemical; D008958:Models, Molecular; D013329:Structure-Activity Relationship; D014357:Trypsin
D004248:DNA (Cytosine-5-)-Methyltransferases; D014357:Trypsin