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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
2000-6-15
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pubmed:abstractText |
The mouse (cytosine-5) DNA methyltransferase (Dnmt1) consists of a regulatory N-terminal and a catalytic C-terminal domain, which are fused by a stretch of Gly-Lys dipeptide repeats. The C-terminal region contains all of the conserved motifs found in other cytosine-5 DNA methyltransferases including the relative position of the catalytic Pro-Cys dipeptide. In prokaryotes, the methyltransferases are simpler and lack the regulatory N-terminal domain. We constructed three hybrid methyltransferases, containing the intact N-terminus of the murine Dnmt1 and most of the coding sequences from M.HhaI (GCGC), M.HpaII (CCGG) or M.SssI (CG). These hybrids are biologically active when expressed in a baculovirus system and show the specificity of the parental C-terminal domain. Expression of these recombinant constructs leads to de novo methylation of both host and viral genomes in a sequence-specific manner. Steady-state kinetic analyses were performed on the murine Dnmt1-HhaI hybrid using poly(dG-dC).poly (dG-dC), unmethylated and hemimethylated oligonucleotides as substrates. The enzyme has a slow catalytic turnover number of 4.38 h(-1) for poly(dG-dC). poly(dG-dC), and exhibits 3-fold higher catalytic efficiency for hemimethylated substrates.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10790376-10551868,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10790376-10551869,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10790376-1368794,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10790376-1423634,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10790376-1594447,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10790376-1628623,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10790376-2651430,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10790376-3210246,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10790376-3558369,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10790376-6357854,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10790376-7502071,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10790376-7629184,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10790376-7980570,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10790376-8127644,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10790376-8293469,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10790376-8392715,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10790376-8652507,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10790376-9302295,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10790376-9358180,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10790376-9451440,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10790376-9628328,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10790376-9628366,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10790376-9662389,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10790376-9755187,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10790376-9847213
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA (Cytosine-5-)-Methyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/DNA modification methylase HhaI,
http://linkedlifedata.com/resource/pubmed/chemical/DNA modification methylase HpaII,
http://linkedlifedata.com/resource/pubmed/chemical/DNA modification methylase SssI,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Cytosine Methylases,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Structural Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/polyhedrin protein...
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
19
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2103-14
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10790376-Amino Acid Motifs,
pubmed-meshheading:10790376-Amino Acid Sequence,
pubmed-meshheading:10790376-Animals,
pubmed-meshheading:10790376-Baculoviridae,
pubmed-meshheading:10790376-Catalytic Domain,
pubmed-meshheading:10790376-DNA,
pubmed-meshheading:10790376-DNA (Cytosine-5-)-Methyltransferase,
pubmed-meshheading:10790376-DNA Methylation,
pubmed-meshheading:10790376-DNA-Cytosine Methylases,
pubmed-meshheading:10790376-Gene Expression Regulation,
pubmed-meshheading:10790376-Genome, Viral,
pubmed-meshheading:10790376-Kinetics,
pubmed-meshheading:10790376-Mice,
pubmed-meshheading:10790376-Molecular Sequence Data,
pubmed-meshheading:10790376-Oligodeoxyribonucleotides,
pubmed-meshheading:10790376-Prokaryotic Cells,
pubmed-meshheading:10790376-Promoter Regions, Genetic,
pubmed-meshheading:10790376-Protein Structure, Tertiary,
pubmed-meshheading:10790376-Recombinant Fusion Proteins,
pubmed-meshheading:10790376-Substrate Specificity,
pubmed-meshheading:10790376-Viral Proteins,
pubmed-meshheading:10790376-Viral Structural Proteins
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pubmed:year |
2000
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pubmed:articleTitle |
Hybrid mouse-prokaryotic DNA (cytosine-5) methyltransferases retain the specificity of the parental C-terminal domain.
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pubmed:affiliation |
New England Biolabs, 32 Tozer Road, Beverly, MA 01915, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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