Histones can be modified by acetylation, methylation, phosphorylation, sumoylation, and ubiquitination.
Histones have N-terminal amino acid tails that protrude and can be modified by acetylation, methylation, ubiquitination, and phosphorylation.
The N-terminal tails of the histones can be modified by acetylation, methylation, phosphorylation, ubiquitination and SUMOylation [ 37], and these post-translational modifications influence gene transcription.
To further investigate the consequence(s) of acetylation on tau, we evaluated the amino acid residues reported to be acetylated by p300, and found all four KXGS motifs in tau's microtubule-binding domain can be modified by acetylation (22).
The identification of tubulin as the first cytosolic protein to be modified by acetylation [ 1, 2] challenged the traditional notion that acetylation only serves as a mechanism to regulate transcription through modification of histones.
Histones can be modified by acetylation, methylation, phosphorylation, sumoylation, and ubiquitination, all of which fine-tune the accessibility of DNA to transcription factors and the subsequent protein interactions that determine chromatin structure.
Endogenous SOD2 is modified by acetylation.
The HDL surface charge was modified by acetylation of protein lysine residues with acetic anhydride.
Histones are proteins that compact DNA in the cell nucleus and are modified by acetylation, methylation, or phosphorylation.
In addition, a recent proteomic study found that many DNA repair proteins including MDC1, BLM, and Rad50 are modified by acetylation after HDAC inhibition (Choudhary et al, 2009).
However, the recent discovery that tau is modified by acetylation necessitates additional research to provide greater mechanistic insight into the spectrum of physiological consequences of tau acetylation, which may hold promise as a novel therapeutic target.
