Structure and nucleosome interaction of the yeast NuA4 and Piccolo-NuA4 histone acetyltransferase complexes

Johnathan R. Chittuluru, Yuriy Chaban, Julie Monnet-Saksouk, Michael J. Carrozza, Vasileia Sapountzi, William Selleck, Jiehuan Huang, Rhea T. Utley, Myriam Cramet, Stephane Allard, Gang Cai, Jerry L. Workman, Michael G. Fried, Song Tan, Jacques Côté, Francisco J. Asturias

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65 Scopus citations


We have used EM and biochemistry to characterize the structure of NuA4, an essential yeast histone acetyltransferase (HAT) complex conserved throughout eukaryotes, and we have determined the interaction of NuA4 with the nucleosome core particle (NCP). The ATM-related Tra1 subunit, which is shared with the SAGA coactivator complex, forms a large domain joined to a second region that accommodates the catalytic subcomplex Piccolo and other NuA4 subunits. EM analysis of a NuA4-NCP complex shows the NCP bound at the periphery of NuA4. EM characterization of Piccolo and Piccolo-NCP provided further information about subunit organization and confirmed that histone acetylation requires minimal contact with the NCP. A small conserved region at the N terminus of Piccolo subunit enhancer of Polycomb-like 1 (Epl1) is essential for NCP interaction, whereas the subunit yeast homolog of mammalian Ing1 2 (Yng2) apparently positions Piccolo for efficient acetylation of histone H4 or histone H2A tails. Taken together, these results provide an understanding of the NuA4 subunit organization and the NuA4-NCP interactions.

Original languageEnglish (US)
Pages (from-to)1196-1203
Number of pages8
JournalNature Structural and Molecular Biology
Issue number11
StatePublished - Nov 2011

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology


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