Linked Life Data

6389549

Source:http://linkedlifedata.com/resource/pubmed/id/6389549

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
23
pubmed:dateCreated
1985-1-10
pubmed:abstractText
A strong correlation has been established between reversible acetylation of histones and transcriptional activation of chromatin. However, the function of histone acetylation remains unknown. We have approached this question by purifying histone acetyltransferase 15,000-fold from yeast and characterizing it enzymatically. Biochemical properties, including the pH and temperature optima and the Michaelis-Menten constants for both acetyl coenzyme A and histones, are similar to those reported for histone acetyltransferases from higher eukaryotes. Yeast histone acetyltransferase has a native molecular weight of 110,000 as determined by gel filtration and is tightly bound to chromatin. It displays high-substrate specificity for histones. It acetylates all four core histones in the order: H4 greater than H2B greater than H2A. 10-fold higher histone acetyltransferase activity is observed for free histones when compared to yeast polynucleosomes as a substrate.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
259
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
14406-12
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Extensive purification and characterization of chromatin-bound histone acetyltransferase from Saccharomyces cerevisiae.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't