Linked Life Data

6272864

Source:http://linkedlifedata.com/resource/pubmed/id/6272864

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1982-2-12
pubmed:abstractText
The nucleotide sequence selectivity of histone binding has been measured by thermal denaturation of reconstituted nucleoproteins. When DNAs of different average base compositions competed for the binding of purified histone fractions during in vitro reconstitutions in the presence of salt and urea, a decreasing (A + T)-binding preference was observed following the order H1 greater than H2B greater than H5 greater than H2A greater than [H2A + H2B] greater than [H2A + H2B + H3 + H4], [H1 + (H2A + H2B + H3 + H4)2]. Nucleoprotein complexes formed under conditions shown to yield more physiologically comparable nucleosome structures revealed a minimal (A + T)-binding preference. These results suggest that homotypic and heterotypic histone interactions decreased the nucleotide sequence selectivity of nucleosome binding.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
656
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
86-92
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Sequence sensitivity of histone binding.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.