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Structure of mouse DNA (cytosine-5-)-methyltransferase.

Abstract
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.
AuthorsE Spiess, A Tomassetti, P Hernaiz-Driever, G P Pfeifer
JournalEuropean journal of biochemistry (Eur J Biochem) Vol. 177 Issue 1 Pg. 29-34 (Oct 15 1988) ISSN: 0014-2956 [Print] England
PMID3141151 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • DNA (Cytosine-5-)-Methyltransferases
  • Trypsin
Topics
  • Animals
  • DNA (Cytosine-5-)-Methyltransferases (analysis)
  • Freeze Drying
  • Mast-Cell Sarcoma (enzymology)
  • Mice
  • Microscopy, Electron
  • Models, Chemical
  • Models, Molecular
  • Structure-Activity Relationship
  • Trypsin

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