Ontology highlight
ABSTRACT:
SUBMITTER: Krogan NJ
PROVIDER: S-EPMC518788 | biostudies-other | 2004 Sep
REPOSITORIES: biostudies-other
Proceedings of the National Academy of Sciences of the United States of America 20040907 37
NuA4, the only essential histone acetyltransferase complex in Saccharomyces cerevisiae, acetylates the N-terminal tails of histones H4 and H2A. Affinity purification of NuA4 revealed the presence of three previously undescribed subunits, Vid21/Eaf1/Ydr359c, Swc4/Eaf2/Ygr002c, and Eaf7/Ynl136w. Experimental analyses revealed at least two functionally distinct sets of polypeptides in NuA4: (i) Vid21 and Yng2, and (ii) Eaf5 and Eaf7. Vid21 and Yng2 are required for bulk histone H4 acetylation and a ...[more]