Linked Life Data

17292837

Source:http://linkedlifedata.com/resource/pubmed/id/17292837

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2007-2-12
pubmed:abstractText
Asf1 is a histone chaperone that favors histone H3/H4 assembly and disassembly. We solved the structure of the conserved domain of human ASF1A in complex with the C-terminal helix of histone H3 using nuclear magnetic resonance spectroscopy. This structure is fully compatible with an association of ASF1 with the heterodimeric form of histones H3/H4. In our model, ASF1 substitutes for the second H3/H4 heterodimer that is normally found in heterotetrameric H3/H4 complexes. This result constitutes an essential step in the fundamental understanding of the mechanisms of nucleosome assembly by histone chaperones. Point mutations that perturb the Asf1/histone interface were designed from the structure. The decreased binding affinity of the Asf1-H3/H4 complex correlates with decreased levels of H3-K56 acetylation and phenotypic defects in vivo.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0969-2126
pubmed:author
pubmed:issnType
Print
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
191-9
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Structure of the histone chaperone ASF1 bound to the histone H3 C-terminal helix and functional insights.
pubmed:affiliation
Institut de Biologie et de Technologie de Saclay, Commissariat à l'Energie Atomique/Saclay, F-91191 Gif-sur-Yvette Cedex, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't