Linked Life Data

1692325

Source:http://linkedlifedata.com/resource/pubmed/id/1692325

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
1990-6-13
pubmed:abstractText
Binding of high mobility group (HMG) proteins 14 and 17 (HMG 14/17) to complete nucleosomal cores and to cores lacking one H2A.H2B dimer, the amino-terminal tails of histones, or both one H2A.H2B dimer and the amino-terminal ends of histones is accompanied by an overall stabilization of the particles as determined by thermal denaturation, circular dichroism and DNase I digestion. In spite of the structural stabilization brought about by HMG 14/17, the presence of these proteins causes little effect on the efficiency of the different nucleosomal particles as transcription templates for RNA polymerase II. The nucleosomal particles lacking one H2A.H2B dimer and containing two bound HMG 14/17 molecules are efficient in vitro transcription templates, which allow transcription of the whole length of the DNA present in the particle. These results are consistent with HMG 14/17 being present in active chromatin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
265
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8225-9
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Structural and transcriptional properties of different nucleosomal particles containing high mobility group proteins 14 and 17 (HMG 14/17).
pubmed:affiliation
Centro de Biología Molecular, Consejo Superior de Investigaciones Científicas, Madrid, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't