The N-terminal tails of histones are subject to multiple covalent modifications that can influence gene expression locally at specific promoters or within large regions of chromatin.
Recent accounts reveal multiple covalent modifications of p53 protein (phosphorylation, acetylation, ribosylation, sumoylation) that alter its stability and its subcellular localization, as well as affecting its ability to bind DNA and transcriptionally activate target genes [ 20].
Four core histones H3, H4, H2A, and H2B comprise the nucleosomal core particle, and each may be decorated with multiple covalent modifications, including acetylation, methylation, phosphorylation, sumoylation, and ubiquitination (Kouzarides, 2007).
Deletion of PhoP/Q-regulated MgrR results in a 10-fold increase in the resistance to polymyxin B. PhoP/Q and PmrA/B are both activated following endocytosis of live S. Typhimurium cells by RAW 264.7 macrophage tumour cells, resulting in multiple partial covalent modifications of lipid A [ 79].
Histone N-terminal tails are subject to multiple covalent post-translational modifications, including lysine (K) acetylation, lysine or arginine (R) methylation, serine (S) phosphorylation, and so on [ 20, 21].
Moreover, the N-termini of histone proteins contain multiple lysine residues and are accessible to covalent modifications such as acetylation, methylation, sumoylation, biotinylation, phosphorylation, glycosylation, and ADP-ribosylation, thus allowing regulation of gene transcription (Fig. 1) [ 4, 5, 33– 33].
This confirmed how close agonist proximity through covalent modifications resulted in contribution from multiple TLR activation pathways, which altered and directed innate immune responses.
Covalent modifications of DNA and proteins by electrophiles produced during oxidative stress have multiple consequences on cellular function, including mutagenesis, stress responses, cellular dysfunction, and ultimately cell death.
Covalent modifications of histones are inherited epigenetically across many generations.
However, Toxoplasma infection prevented these covalent modifications.
Covalent modifications of histones (acetylation, methylation, phosphorylation, ubiquitination, etc).
