MCB Accepts, published online ahead of print on 12 October 2009

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Mol. Cell. Biol. doi:10.1128/MCB.01033-09
Copyright (c) 2009, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

The NuA4 lysine acetyltransferase Esa1 is targeted to coding regions and stimulates transcription elongation with Gcn5

Daniel S. Ginsburg, Chhabi K. Govind, and Alan G. Hinnebusch^*

Laboratory of Gene Regulation and Development, National Institute of Child Health and Human Development, Bethesda, MD 20892

^* To whom correspondence should be addressed. Email: ahinnebusch{at}nih.gov.

NuA4, the major H4 acetyltransferase (KAT) complex in budding yeast, is recruited to promoters and stimulates transcription initiation. NuA4 subunits contain domains that bind methylated histones, suggesting that histone methylation should target NuA4 to coding sequences during transcription elongation. We show that NuA4 is co-transcriptionally recruited dependent on its physical association with elongating Pol II phosphorylated on the CTD by CDK7/Kin28, but independent of subunits (Eaf1 and Tra1) required for NuA4 recruitment to promoters. Whereas histone methylation by Set1 and Set2 is dispensable for NuA4's interaction with Pol II and targeting to some coding regions, it stimulates NuA4-histone interaction and H4 acetylation in vivo. The NuA4 KAT, Esa1, mediates increased H4 acetylation, enhanced RSC occupancy and histone eviction in coding sequences, and stimulates the rate of transcription elongation. Esa1 cooperates with the H3 KAT in SAGA, Gcn5, to enhance these functions. Our findings delineate a pathway for acetylation-mediated nucleosome remodeling and eviction in coding sequences that stimulates transcription elongation by Pol II in vivo.