SnapShot: Lysine Methylation beyond Histones

Lysine methylation: beyond histones.

Posttranslational modifications (PTMs) of histone proteins, such as acetylation, methylation, phosphorylation, and ubiquitylation, play essential roles in regulating chromatin dynamics. Combinations of different modifications on the histone proteins, termed 'histone code' in many cases, extend the information potential of the genetic code by regulating DNA at the epigenetic level. Many PTMs occ...

Histones with High Lysine Content

1. The preparation and properties of lysine-rich histones, which differ in a number of respects from the classical arginine-rich histones, have been described. 2. Lysine-rich histones, like those previously known, are located in cell nuclei. 3. Lysine-rich histones dissociate more readily from combination with nucleic acid than do other histones.

SnapShot: Histone Lysine Methylase Complexes

Invited Review HDAC8 Substrates: Histones and Beyond

A cetylation of lysine side chains in proteins is a reversible post-translational modification that occurs in a wide range of organisms. This modification affects the properties of proteins, including protein–protein association, protein–DNA interactions, and protein stability. Initially, acetylation gained recognition as a post-translational modification to histones. Acetylation of histones ca...

Species and organ specificity in very lysine-rich histones.

Very lysine-rich histones were extracted by aqueous trichloracetic acid from calf thymus, from the thymus, mammary gland, and liver of rabbits, and from chicken livers. The elution profiles of these histones, obtained by chromatography on Amberlite IRC-50 with a shallow guanidinium chloride gradient, revealed that the very lysine-rich histone complement varied from one animal species to another...