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J. Biol. Chem., Vol. 276, Issue 21, 18605-18613, May 25, 2001
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From the Institute of Biosciences and Technology, Center for Genome
Research, Texas A & M University System Health Science Center, Texas
Medical Center, Houston, Texas 77030-3303 and Steady-state kinetic analyses revealed that the
methylation reaction of the human DNA (cytosine-5) methyltransferase 1 (DNMT1) is repressed by the N-terminal domain comprising the first 501 amino acids, and that repression is relieved when methylated DNA binds
to this region. DNMT1 lacking the first 501 amino acids retains its
preference for hemimethylated DNA. The methylation reaction proceeds by
a sequential mechanism, and either substrate (S-adenosyl-L-methionine and unmethylated DNA)
may be the first to bind to the active site. However, initial binding
of S-adenosyl-L-methionine is preferred. The
binding affinities of DNA for both the regulatory and the catalytic
sites increase in the presence of methylated CpG dinucleotides and vary
considerably (more than one hundred times) according to DNA sequence.
DNA topology strongly influences the reaction rates, which increased
with increasing negative superhelical tension. These kinetic data are
consistent with the role of DNMT1 in maintaining the methylation
patterns throughout development and suggest that the enzyme may be
involved in the etiology of fragile X, a syndrome characterized by
de novo methylation of a greatly expanded CGG·CCG triplet
repeat sequence.
Recombinant Human DNA (Cytosine-5) Methyltransferase
III. ALLOSTERIC CONTROL, REACTION ORDER, AND INFLUENCE OF
PLASMID TOPOLOGY AND TRIPLET REPEAT LENGTH ON METHYLATION OF THE
FRAGILE X CGG·CCG SEQUENCE*
,, and New
England Biolabs, Beverly, Massachusetts 01915
*
This work was supported by National Institutes of Health
Grants GM46127 (to R. J. R.), GM52982, and NS37554 (to R. D. W.), the Robert A. Welch Foundation, and Polycystic Kidney Research Foundation Grant 99004 (to R. D. W.). This paper is the third in a
series on human DNA (cytosine-5) methyltransferase. Papers I and II
appeared in J. Biol. Chem. 274, 33002-33010 and 33011-33019.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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