SGD Paper 
Garcia BA, et al. (2007) Organismal differences in post-translational modifications in histones H3 and H4. J Biol Chem 282(10):7641-55
Abstract: Post-translational modifications (PTMs) of histones play an important role in many cellular processes, notably gene regulation. Using a combination of mass spectrometric and immuno-biochemical approaches, we show that the PTM profile of histone H3 differs significantly among the various model organisms examined. Unicellular eukaryotes, such as S. cerevisiae (yeast) and Tetrahymena thermophila (Tet), for example, contain more activation than silencing marks as compared to mammalian cells (mouse and human), which are generally enriched in PTMs more often associated with gene silencing. Close examination reveals that many of the better-known modified lysines (K) can be either methylated or acetylated and that the overall modification patterns become more complex from unicellular eukaryotes to mammals. Additionally, novel species-specific H3 PTMs from wild-type asynchronously-grown cells are also detected by mass spectrometry. Our results suggest that some PTMs are more conserved than previously thought, including H3K9me1 and H4K20me2 in yeast and H3K27me1, me2, me3 in Tet. On histone H4, methylation at K20 showed a similar pattern as H3 methylation at K9, with mammals containing more methylation than the unicellular organisms. Additionally, modification profiles of H4 acetylation were very similar among the organisms examined, suggesting that the more complex and species-specific PTM patterns observed on H3 might have originated from the development of additional enzyme systems that govern the steady-state balance of these marks and from the presence of more H3 variants in mammals.
| Status: Published | Type: Journal Article | PubMed ID: 17194708 |
Topics addressed in this paper
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