rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2006-8-4
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pubmed:abstractText |
Effective methods of probing chromatin structure without disrupting DNA-protein interactions and associations are necessary for creating an accurate picture of chromatin and its processes in vivo. Expression of cytidine-5 DNA methyltransferases (C5 DMTases) in Saccharomyces cerevisiae provides a powerful noninvasive method of assaying relative DNA accessibility in chromatin. DNA MTases are occluded from protein-associated DNA based on the strength and span of the DNA-protein interaction. Ectopic regulation of C5 DMTase expression systems allows for minimal disruption of yeast physiology. Methylated sites are detected by bisulfite genomic sequencing, which leads to a positive signal corresponding to modified cytidine residues. High-resolution C5 DMTases with dinucleotide recognition specificity are shown to provide sufficient coverage to map interactions spanning a relatively short distance.
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pubmed:grant |
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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 |
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pubmed:status |
MEDLINE
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pubmed:issn |
1064-3745
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
338
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
225-44
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:16888362-Base Sequence,
pubmed-meshheading:16888362-Chromatin,
pubmed-meshheading:16888362-DNA,
pubmed-meshheading:16888362-DNA, Fungal,
pubmed-meshheading:16888362-DNA (Cytosine-5-)-Methyltransferase,
pubmed-meshheading:16888362-DNA Primers,
pubmed-meshheading:16888362-Escherichia coli,
pubmed-meshheading:16888362-Molecular Probe Techniques,
pubmed-meshheading:16888362-Nuclear Proteins,
pubmed-meshheading:16888362-Polymerase Chain Reaction,
pubmed-meshheading:16888362-Protein Binding,
pubmed-meshheading:16888362-Recombinant Proteins,
pubmed-meshheading:16888362-Saccharomyces cerevisiae,
pubmed-meshheading:16888362-Transformation, Genetic
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pubmed:year |
2006
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pubmed:articleTitle |
DNA methyltransferase probing of DNA-protein interactions.
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pubmed:affiliation |
Department of Biochemistry and Biophysics, Texas A & M University, College Station, TX, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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