Biotinylation is a natural, albeit rare, modification of human histones

A novel, enigmatic histone modification: biotinylation of histones by holocarboxylase synthetase.

Holocarboxylase synthetase catalyzes the covalent binding of biotin to histones in humans and other eukaryotes. Eleven biotinylation sites have been identified in histones H2A, H3, and H4. K12-biotinylated histone H4 is enriched in heterochromatin, repeat regions, and plays a role in gene repression. About 30% of the histone H4 molecules are biotinylated at K12 in histone H4 in human fibroblast...

Modification of Histones during Spermatogenesis in Trout

Trout testis cells were incubated with 13H]arginine and lysine and inorganic [32P]phosphate. Histones were extracted with acid and the major fractions (I, IIbl, IIb2, III monomer, and IV) were resolved by chromatography on BioGel P-10. The profile of 32P incorporation was time dependent. When the phosphorylated histones in each of the major fractions were resolved from unphosphorylated species ...

Is esophageal atresia a natural way of fasting?

Exposure to UV light causes increased biotinylation of histones in Jurkat cells.

Biotin in breakdown products of biotinylated carboxylases serves as substrate for biotinylation of histones by biotinidase. Here we determined whether biotinylation of histones might play a role in repair of damaged DNA and in apoptosis. Jurkat cells were exposed to UV light to induce DNA damage. Abundance of thymine dimers increased about three times in response to UV exposure, consistent with...

Chromatin modification: How to put a HAT on the histones

Specific patterns of acetylation of the core histones are associated with specific structures and functions of chromatin. A basis for the specificity of acetylation is now apparent in the recent crystal structures of two acetyltransferases.