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RESEARCH PAPER
1 Laval University Cancer Research Center, Hôtel-Dieu de Québec (CHUQ), Quebec City, Qc G1R 2J6 Canada; 2 Center for Gene Regulation, Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, USA; 3 Harvard Microchemistry Facility, Harvard University, Cambridge, Massachusetts 02138, USA
Drosophila Enhancer of Polycomb, E(Pc), is a suppressor of position-effect variegation and an enhancer of both Polycomb and trithorax mutations. A homologous yeast protein, Epl1, is a subunit of the NuA4 histone acetyltransferase complex. Epl1 depletion causes cells to accumulate in G2/M and global loss of acetylated histones H4 and H2A. In relation to the Drosophila protein, mutation of Epl1 suppresses gene silencing by telomere position effect. Epl1 protein is found in the NuA4 complex and a novel highly active smaller complex named Piccolo NuA4 (picNuA4). The picNuA4 complex contains Esa1, Epl1, and Yng2 as subunits and strongly prefers chromatin over free histones as substrate. Epl1 conserved N-terminal domain bridges Esa1 and Yng2 together, stimulating Esa1 catalytic activity and enabling acetylation of chromatin substrates. A recombinant picNuA4 complex shows characteristics similar to the native complex, including strong chromatin preference. Cells expressing only the N-terminal half of Epl1 lack NuA4 HAT activity, but possess picNuA4 complex and activity. These results indicate that the essential aspect of Esa1 and Epl1 resides in picNuA4 function. We propose that picNuA4 represents a nontargeted histone H4/H2A acetyltransferase activity responsible for global acetylation, whereas the NuA4 complex is recruited to specific genomic loci to perturb locally the dynamic acetylation/deacetylation equilibrium.
[Keywords: Chromatin acetylation; histone H4; NuA4 complex; Epl1; Esa1; Yng2]
Received November 12, 2002; revised version accepted April 4, 2003.
5 E-MAIL jacques.cote{at}crhdq.ulaval.ca; FAX (418) 691-5439.
Article and publication are at http://www.genesdev.org/cgi/doi/10.1101/gad.1056603.
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