Linked Life Data

2760072

Source:http://linkedlifedata.com/resource/pubmed/id/2760072

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
1989-9-13
pubmed:abstractText
Histone proteins, which were assembled into chromatin using the Xenopus oocyte S-150 extract, were analyzed on acid-urea gels and Triton-acid-urea gels to determine their state of modification. We find that histone H4, which is present in a diacetylated form in the oocyte S-150, gradually loses its acetate groups as the DNA is packaged into chromatin. Thus, this process parallels the one observed in vivo during chromatin formation in growing eucaryotic cells. Histone H4 deacetylation in the oocyte S-150 is a DNA-dependent reaction. This reaction is blocked when butyrate (an inhibitor of histone deacetylase) is added at the onset of the chromatin assembly process. When butyrate is added at the end of the assembly process, no de novo acetylation of the nucleosomal histone H4 is observed. Chromatin with regularly spaced nucleosomes, displaying periodicities ranging from 160 to 220 base pairs, can be assembled in vitro with the oocyte S-150 (Rodríguez-Campos, A., Shimamura, A., and Worcel, A. (1989) J. Mol. Biol., in press). This chromatin may contain either deacetylated histone H4 when assembled under standard conditions or diacetylated H4 when assembled in the presence of butyrate. Both types of chromatin display identical structures upon digestion with nucleases. The potential applications of this system toward the study of the naturally occurring diacetylated histone H4 are discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
264
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
14524-30
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
The assembly of regularly spaced nucleosomes in the Xenopus oocyte S-150 extract is accompanied by deacetylation of histone H4.
pubmed:affiliation
Department of Biology, University of Rochester, New York 14627.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.