Linked Life Data

3254163

Source:http://linkedlifedata.com/resource/pubmed/id/3254163

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1989-8-18
pubmed:abstractText
When chromatin matrix, "stripped" from its loosely-bound components by extraction with 3 M NaCl, is extensively digested with DNAase I, a fraction is obtained, which carries no endogenous DNA methyltransferase activity but which is a good substrate for externally added enzyme. Under the same conditions, protein-free DNA isolated from this fraction can instead hardly be methylated, this different behaviour pointing to a role of DNA-tightly-bound proteins in favoring or promoting the catalytic action of the enzyme. A similar stimulation of enzymatic methylation could also be shown when, in the presence of this same fraction, single stranded Micrococcus luteus DNA was incubated with placental methyltransferase, using S-adenosylmethionine as a methyl donor. This finding can be correlated to the existence, in chromatin loops, of small regions which resist digestion by DNAase I also after high-salt removal of their loosely-bound components (presumably because of the presence of tightly-bound proteins) and whose DNA is characterized by high methylation levels and, at the same time, by high relative content of thymine.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0158-5231
pubmed:author
pubmed:issnType
Print
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
863-75
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Do tightly-bound chromatin proteins play a role in DNA methylation?
pubmed:affiliation
Dipartimenti di Scienze Biochimiche, Università di Roma La Saplenza, Italy.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't