Exchange of associated factors directs a switch in HBO1 acetyltransferase histone tail specificity

Marie Eve Lalonde, Nikita Avvakumov, Karen C. Glass, France Hélène Joncas, Nehmé Saksouk, Michael Holliday, Eric Paquet, Kezhi Yan, Qiong Tong, Brianna J. Klein, Song Tan, Xiang Jiao Yang, Tatiana G. Kutateladze, Jacques Côté

Research output: Contribution to journalArticlepeer-review

121 Scopus citations


Histone acetyltransferases (HATs) assemble into multisubunit complexes in order to target distinct lysine residues on nucleosomal histones. Here, we characterize native HAT complexes assembled by the BRPF family of scaffold proteins. Their plant homeodomain (PHD)-Zn knuckle-PHD domain is essential for binding chromatin and is restricted to unmethylated H3K4, a specificity that is reversed by the associated ING subunit. Native BRPF1 complexes can contain either MOZ/MORF or HBO1 as catalytic acetyltransferase subunit. Interestingly, while the previously reported HBO1 complexes containing JADE scaffold proteins target histone H4, the HBO1-BRPF1 complex acetylates only H3 in chromatin. We mapped a small region to the N terminus of scaffold proteins responsible for histone tail selection on chromatin. Thus, alternate choice of subunits associated with HBO1 can switch its specificity between H4 and H3 tails. These results uncover a crucial new role for associated proteins within HAT complexes, previously thought to be intrinsic to the catalytic subunit.

Original languageEnglish (US)
Pages (from-to)2009-2024
Number of pages16
JournalGenes and Development
Issue number18
StatePublished - Sep 2013

All Science Journal Classification (ASJC) codes

  • Genetics
  • Developmental Biology


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