Asf1-like structure of the conserved Yaf9 YEATS domain and role in H2A.Z deposition and acetylation

Alice Y. Wang, Julia M. Schulze, Emmanuel Skordalakes, Jennifer W. Gin, James M. Berger, Jasper Rine, Michael S. Kobor

Research output: Contribution to journalArticlepeer-review


Chromatin can be modified by posttranslational modifications of histones, ATP-dependent remodeling, and incorporation of histone variants. The Saccharomyces cerevisiae protein Yaf9 is a subunit of both the essential histone acetyltransferase complex NuA4 and the ATP-dependent chromatin remodeling complex SWR1-C, which deposits histone variant H2A.Z into euchromatin. Yaf9 contains a YEATS domain, found in proteins associated with multiple chromatin-modifying enzymes and transcription complexes across eukaryotes. Here, we established the conservation of YEATS domain function from yeast to human, and determined the structure of this region from Yaf9 by x-ray crystallography to 2.3 Å resolution. The Yaf9 YEATS domain consisted of a β-sandwich characteristic of the Ig fold and contained three distinct conserved structural features. The structure of the Yaf9 YEATS domain was highly similar to that of the histone chaperone Asf1, a similarity that extended to an ability of Yaf9 to bind histones H3 and H4 in vitro. Using structure-function analysis, we found that the YEATS domain was required for Yaf9 function, histone variant H2A.Z chromatin deposition at specific promoters, and H2A.Z acetylation.

Original languageEnglish (US)
Pages (from-to)21573-21578
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number51
StatePublished - Dec 22 2009
Externally publishedYes


  • Chromatin
  • GAS41
  • Histone variants
  • NuA4
  • SWR1-C

ASJC Scopus subject areas

  • General


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