Linked Life Data

3513841

Source:http://linkedlifedata.com/resource/pubmed/id/3513841

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2-3
pubmed:dateCreated
1986-4-29
pubmed:abstractText
We have characterized a histone deacetylase activity associated with yeast nuclei. An unusual feature of the deacetylase is that it is not inhibited by the short-chain fatty acids n-butyrate and propionate. These short-chain fatty acids are typically potent inhibitors of histone deacetylases in eukaryotic systems. The deacetylase(s) were detected by monitoring the levels of acetylation of yeast histones during incubation of isolated yeast nuclei. The activity was optimal at 37 degrees C and at 0.1 M NaCl. The enzyme did not require divalent cations and was inhibited by Zn2+ and Cu2+. A simple activity assay was developed using as substrate, [3H]acetate-labeled histone in chicken erythrocyte nuclei. This assay was used to demonstrate that the deacetylase(s) can be extracted from yeast nuclei with 0.5 M NaCl. A gel electrophoretic analysis of the deacetylated chicken histones verified that the solubilization of incorporated radiolabel was a result of histone deacetylation, not an artifact of histone degradation by yeast proteinases.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
866
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
161-9
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
A novel yeast histone deacetylase: partial characterization and development of an activity assay.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't