Linked Life Data

17292837

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

Statements in which the resource exists.
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pubmed-article:17292837pubmed:abstractTextAsf1 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.lld:pubmed
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pubmed-article:17292837pubmed:articleTitleStructure of the histone chaperone ASF1 bound to the histone H3 C-terminal helix and functional insights.lld:pubmed
pubmed-article:17292837pubmed:affiliationInstitut de Biologie et de Technologie de Saclay, Commissariat à l'Energie Atomique/Saclay, F-91191 Gif-sur-Yvette Cedex, France.lld:pubmed
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