Characterization of lysine 56 of histone H3 as an acetylation site in Saccharomyces cerevisiae

Anil Ozdemir, Salvatore Spicuglia, Edwin Lasonder, Michiel Vermeulen, Coen Campsteijn, Hendrik G. Stunnenberg, Colin Logie*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

100 Citations (Scopus)
4 Downloads (Pure)


Post-translational histone modifications abound and regulate multiple nuclear processes. Most modifications are targeted to the amino-terminal domains of histones. Here we report the identification and characterization of acetylation of lysine 56 within the core domain of histone H3. In the crystal structure of the nucleosome, lysine 56 contacts DNA. Phenotypic analysis suggests that lysine 56 is critical for histone function and that it modulates formamide resistance, ultraviolet radiation sensitivity, and sensitivity to hydroxyurea. We show that the acetylated form of histone H3 lysine 56 (H3-K56) is present during interphase, metaphase, and S phase. Finally, reverse genetic analysis indicates that none of the known histone acetyltransferases is solely responsible for H3-K56 acetylation in Saccharomyces cerevisiae.

Original languageEnglish
Pages (from-to)25949-25952
Number of pages4
JournalJournal of Biological Chemistry
Issue number28
Publication statusPublished - 15 Jul 2005
Externally publishedYes


Dive into the research topics of 'Characterization of lysine 56 of histone H3 as an acetylation site in Saccharomyces cerevisiae'. Together they form a unique fingerprint.

Cite this