Nucleic Acids Research, Vol 25, Issue 12 2375-2380, Copyright © 1997 by Oxford University Press
M Fremont, M Siegmann, S Gaulis, R Matthies, D Hess and JP Jost
We have previously purified and characterized a 5-methylcytosine (5-
MeC)-DNA glycosylase from 12 day old chick embryos [Jost,J.P. et al. (1995)
J. Biol. Chem. 270, 9734-9739]. The activity of the purified enzyme is
abolished upon treatment with proteinase K and ribonuclease A. RNA
copurifies with 5-MeC-DNA glycosylase activity throughout all
chromatographic steps and preparative gel electrophoresis. RNA with a
length of approximately 300-500 nucleotides was isolated from the gel
purified enzyme. Upon extensive treatment with proteinase K, the gel eluted
and labeled RNA did not show any significant change in molecular mass. The
purified RNA incubated alone or in the presence of Mg2+and
deoxyribonucleotide phosphates had no 5-MeC-DNA glycosylase or
demethylating activities. However, activity of 5-MeC-DNA glycosylase could
be restored when the purified RNA was incubated with the inactive protein,
free of RNA.
ARTICLES
Demethylation of DNA by purified chick embryo 5-methylcytosine-DNA glycosylase requires both protein and RNA
Friedrich Miescher Institute, PO Box 2543, CH-4002 Basel, Switzerland.
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