Following the identification of histone H3 modifications in Saccharomyces cerevisiae [K. Zhang, Int. J. Mass Spectrom. 269 (2008) 101-111], here, we report a detailed characterization of post-translational modifications by LC/MS/MS analysis of tryptic and Glu-C digests of H2B proteins isolated from S. cerevisiae. We show that both H2B.1 and H2B.2 are acetylated at K6, K11, K16, K21 and K22 while H2B.2 has an additional acetylation site at K3. All the acetylation sites of yeast H2B except K3 of H2B.2 are located at the same positions on aligned protein sequences of Arabidopsis H2B variants that were reported previously to be acetylated at K6, K11, K27, K32, K38 and K39. A unique acetylation motif AEK is observed in the H2B variants of these two species, indicating a plant/yeast H2B specific acetyltransferase may exist.
- Histone H2B
- Mass spectrometry
- Post-translational modification (PTM)
ASJC Scopus subject areas
- Condensed Matter Physics
- Physical and Theoretical Chemistry