Distinct domains in high mobility group N variants modulate specific chromatin modifications.
We have demonstrated that levels of specific modification in histone H3 are modulated by members of the nucleosome-binding high mobility group N (HMGN) protein family in a variant-specific manner. HMGN1 (but not HMGN2) inhibits the phosphorylation of both H3S10 and H3S28, whereas HMGN2 enhances H3K14 acetylation more robustly than HMGN1. Two HMGN domains are necessary for modulating chromatin modifications, a non-modification-specific domain necessary for chromatin binding and a modification-specific domain localized in the C terminus of the HMGNs. Thus, chromatin-binding structural proteins such as HMGNs affect the levels of specific chromatin modifications and therefore may play a role in epigenetic regulation.
Protein Section, Laboratory of Metabolism, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Tetsuya
T
Ueda
Yuri V
YV
Postnikov
Michael
M
Bustin
D000107:Acetylation; D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism; D002645:Chickens; D002843:Chromatin / Q000737:chemistry* / Q000378:metabolism; D002875:Chromosomes / Q000378:metabolism; D044127:Epigenesis, Genetic; D004912:Erythrocytes / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D005786:Gene Expression Regulation; D024241:HMGN1 Protein / Q000737:chemistry; D024242:HMGN2 Protein / Q000737:chemistry; D006609:High Mobility Group Proteins / Q000737:chemistry; D051548:Histone Acetyltransferases / Q000737:chemistry; D006657:Histones / Q000737:chemistry; D009154:Mutation; D009707:Nucleosomes / Q000737:chemistry / Q000378:metabolism; D010766:Phosphorylation; D011485:Protein Binding; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D013997:Time Factors
D002843:Chromatin; D024241:HMGN1 Protein; D024242:HMGN2 Protein; D006609:High Mobility Group Proteins; D006657:Histones; D009707:Nucleosomes; D051548:Histone Acetyltransferases