Genomic characterization reveals a simple histone H4 acetylation code
Citations Over TimeTop 1% of 2005 papers
Abstract
The histone code hypothesis holds that covalent posttranslational modifications of histone tails are interpreted by the cell to yield a rich combinatorial transcriptional output. This hypothesis has been the subject of active debate in the literature. Here, we investigated the combinatorial complexity of the acetylation code at the four lysine residues of the histone H4 tail in budding yeast. We constructed yeast strains carrying all 15 possible combinations of mutations among lysines 5, 8, 12, and 16 to arginine in the histone H4 tail, mimicking positively charged, unacetylated lysine states, and characterized the resulting genome-wide changes in gene expression by using DNA microarrays. Only the lysine 16 mutation had specific transcriptional consequences independent of the mutational state of the other lysines (affecting approximately 100 genes). In contrast, for lysines 5, 8, and 12, expression changes were due to nonspecific, cumulative effects seen as increased transcription correlating with an increase in the total number of mutations (affecting approximately 1,200 genes). Thus, acetylation of histone H4 is interpreted by two mechanisms: a specific mechanism for lysine 16 and a nonspecific, cumulative mechanism for lysines 5, 8, and 12.
Related Papers
- → Intra- and inter-nucleosomal interactions of the histone H4 tail revealed with a human nucleosome core particle with genetically-incorporated H4 tetra-acetylation(2015)84 cited
- → Reduce, Retain, Recycle: Mechanisms for Promoting Histone Protein Degradation versus Stability and Retention(2021)20 cited
- → The conformational flexibility of the C-terminus of histone H4 promotes histone octamer and nucleosome stability and yeast viability(2012)23 cited
- → Effects of Sin- versions of histone H4 on yeast chromatin structure and function(1997)79 cited
- Cell cycle dependent phosphorylation of histone H1 in Epstein-Barr virus-transformed B cells(2006)