Chromatin domain boundaries delimited by a histone-binding protein in yeast.

Détails

ID Serval
serval:BIB_5062161CA23C
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Chromatin domain boundaries delimited by a histone-binding protein in yeast.
Périodique
Journal of Biological Chemistry
Auteur(s)
Ferrari S., Simmen K.C., Dusserre Y., Müller K., Fourel G., Gilson E., Mermod N.
ISSN
0021-9258[print], 0021-9258[linking]
Statut éditorial
Publié
Date de publication
12/2004
Volume
279
Numéro
53
Pages
55520-55530
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
When located next to chromosomal elements such as telomeres, genes can be subjected to epigenetic silencing. In yeast, this is mediated by the propagation of the SIR proteins from telomeres toward more centromeric regions. Particular transcription factors can protect downstream genes from silencing when tethered between the gene and the telomere, and they may thus act as chromatin domain boundaries. Here we have studied one such transcription factor, CTF-1, that binds directly histone H3. A deletion mutagenesis localized the barrier activity to the CTF-1 histone-binding domain. A saturating point mutagenesis of this domain identified several amino acid substitutions that similarly inhibited the boundary and histone binding activities. Chromatin immunoprecipitation experiments indicated that the barrier protein efficiently prevents the spreading of SIR proteins, and that it separates domains of hypoacetylated and hyperacetylated histones. Together, these results suggest a mechanism by which proteins such as CTF-1 may interact directly with histone H3 to prevent the propagation of a silent chromatin structure, thereby defining boundaries of permissive and silent chromatin domains.
Mots-clé
Animals, Blotting, Western, CCAAT-Enhancer-Binding Proteins/chemistry, Chromatin/chemistry, Chromatin/metabolism, Chromatin Immunoprecipitation, Chromosomes/ultrastructure, DNA/chemistry, DNA/metabolism, Fungal Proteins/chemistry, Fungal Proteins/metabolism, Gene Deletion, Gene Silencing, Genes, Reporter, Genetic Vectors, Histones/chemistry, Immunoprecipitation, Mice, Models, Biological, Models, Genetic, Mutagenesis, Mutation, NFI Transcription Factors, NIH 3T3 Cells, Point Mutation, Protein Binding, Protein Structure, Tertiary, Telomere/ultrastructure, Transcription Factors/chemistry, Transcription, Genetic, Transcriptional Activation, Transfection, Transforming Growth Factor beta/metabolism, Two-Hybrid System Techniques
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 10:41
Dernière modification de la notice
20/08/2019 14:06
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