Cracking the enigmatic linker histone code.
Recently, the existence of a 'histone code' has been proposed to explain the link between the covalent chemical modification of histone proteins and the epigenetic regulation of gene activity. Although the role of the four 'core' histones has been extensively studied, little is known about the involvement of the linker histone, histone H1 and its variants, in this code. For many years, few sites of chemical modification had been mapped in linker histones, but this has changed recently with the use of functional proteomic techniques, principally mass spectrometry, to characterize these modifications. The functionality of many of these sites, however, remains to be determined.
Godde
James S
JS
Division of Gene Therapy Science, Osaka University Graduate School of Medicine, 2-2 Yamada-oka, Suita, Osaka, Japan.
Ura
Kiyoe
K
D000818:Animals; D005057:Eukaryotic Cells / Q000378:metabolism; D017353:Gene Deletion; D042421:Histone Code; D006657:Histones / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D013058:Mass Spectrometry; D011499:Protein Processing, Post-Translational
D006657:Histones