Two-Color Cell Array Screen Reveals Interdependent Roles for Histone Chaperones and a Chromatin Boundary Regulator in Histone Gene Repression
| Autor: | Lourdes Peña-Castillo, Jack Greenblatt, Timothy P. Hughes, Corey Nislow, Jeffrey Fillingham, Harm van Bakel, Jean-Philippe Lambert, Brenda J. Andrews, Daniel Figeys, Pinay Kainth, Kyle Tsui |
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| Rok vydání: | 2009 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Chromosomal Proteins Non-Histone Cell Cycle Proteins Saccharomyces cerevisiae Biology SAP30 Chromatin remodeling Histones Histone H1 Genes Reporter Histone methylation Histone H2A Histone code Promoter Regions Genetic Molecular Biology Histone Acetyltransferases Genetics Nuclear Proteins Genomics Cell Biology Cell biology Repressor Proteins Gene Expression Regulation Histone methyltransferase Genome Fungal Chromatin immunoprecipitation Molecular Chaperones |
| Zdroj: | Molecular Cell. 35(3):340-351 |
| ISSN: | 1097-2765 |
| DOI: | 10.1016/j.molcel.2009.06.023 |
| Popis: | We describe a fluorescent reporter system that exploits the functional genomic tools available in budding yeast to systematically assess consequences of genetic perturbations on gene expression. We used our Reporter-Synthetic Genetic Array (R-SGA) method to screen for regulators of core histone gene expression. We discovered that the histone chaperone Rtt106 functions in a pathway with two other chaperones, Asf1 and the HIR complex, to create a repressive chromatin structure at core histone promoters. We found that activation of histone (HTA1) gene expression involves both relief of Rtt106-mediated repression by the activity of the histone acetyltransferase Rtt109 and restriction of Rtt106 to the promoter region by the bromodomain-containing protein Yta7. We propose that the maintenance of Asf1/HIR/Rtt106-mediated repressive chromatin domains is the primary mechanism of cell-cycle regulation of histone promoters. Our data suggest that this pathway may represent a chromatin regulatory mechanism that is broadly used across the genome. |
| Databáze: | OpenAIRE |
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