Linked Life Data

7893706

Source:http://linkedlifedata.com/resource/pubmed/id/7893706

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1995-4-21
pubmed:abstractText
In the following report the relationship between histone methylation and histone acetylation has been examined in HeLa cells to better define the distribution of these two modifications. By labeling methylated histones in the presence or absence of sodium butyrate, we have found that the methylation of H3 is much more targeted to rapidly acetylated chromatin than is the methylation of H4, which largely involves the unacetylated subtype even in the presence of butyrate. Newly methylated H3 is highly likely to be complexed in nucleosomes that contain acetylated H4, as determined by immunoprecipitating radiolabeled chromatin with antibodies specific for acetylated H4 isoforms. In contrast, dynamically methylated H4 is underrepresented in acetylated chromatin, relative to newly methylated H3. The preferential methylation of acetylated H3 continues after pretreatment of cells with cycloheximide, indicating that not all acetylation-related methylation is associated with histone synthesis. This was confirmed by analyzing histone methylation in cells arrested at the G1/S boundary, in which histone synthesis was sharply lowered (relative to randomly cycling cells): under these conditions H3 methylation declined only approximately 4-fold, although ongoing methylation of H4 decreased approximately 20-fold. The continuing methylation of H3 in arrested cells included all H3 sequence variants, was selective for acetylated H3, and coincided with methyl group turnover that could not be ascribed to histone replacement synthesis. Most newly methylated H3 in arrested cells was complexed with acetylated H4 in chromatin.(ABSTRACT TRUNCATED AT 250 WORDS)
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
34
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2916-24
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Relationship between methylation and acetylation of arginine-rich histones in cycling and arrested HeLa cells.
pubmed:affiliation
Department of Biology, Boston College, Chestnut Hill, Massachusetts 02167.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't