Non-enzymatic glycation of histones

Abstract

2-(2-Furoyl)-5-(2-furanyl)-1H-imidazole (FFI) is detected in total histones and the lysine-rich histone 1 fraction isolated from calf thymus after in vitro glycation and hydrolysis with HCl, using gas chromatographic/mass spectrometric analysis. The finding suggests that glucose is bound to the epsilon-amino groups of the lysine residues of the histones. No FFI is monitored in native histone samples.

Glycoxidation of histone proteins in autoimmune disorders

“…The term 'glycohistone' was coined by Jobst et al in 1991 after they detected histone glycation in hepatic nuclei of patients dying of decompensated diabetes [34]. They attempted to explain the terms of interaction of histone proteins and sugars by kinetic studies of histone protein glycation [35,36].…”

The key to development: interpreting the histone code?

“…The amino termini of histones (histone tails) are accessible, unstructured domains that protrude out of the nucleosomes. Histones, especially residues of the amino termini of histones H3 and H4 and the amino and carboxyl termini of histones H2A, H2B and H1, are susceptible to a variety of post-translational modifications ( Figure 1): phosphorylation (of S and T residues) [4]; acetylation (K) [5,6]; methylation (K and R) [7]; ubiquitination (K) [8]; sumoylation (K) [9]; ADP ribosylation [10]; glycosylation [11]; biotinylation [12], and carbonylation [13]. Although the first three types of modifications have been studied extensively [14], relatively little is known about the others.…”

Evidence for the implication of the histone code in building the genome structure

“…Over the course of the last decade, amino acids have been shown to experience several modifications, of at least twelve types: acetylation (lysine), methylation (lysine and arginine), phosphorylation (serine and threonine), sumoylation (lysine), ubiquitylation (lysine), ADP ribosylation, butyrylation, citrullination, crotonylation, formylation, proline isomerization, propionylation [34][35][36][37][38][39].…”