title: Chromosomal protein HMGN1 enhances the acetylation of lysine 14 in histone H3.
abstract: The acetylation levels of lysine residues in nucleosomes, which are determined by the opposing activities of histone acetyltransferases (HATs) and deacetylases, play an important role in regulating chromatin-related processes, including transcription. We report that HMGN1, a nucleosomal binding protein that reduces the compaction of the chromatin fiber, increases the levels of acetylation of K14 in H3. The levels of H3K14ac in Hmgn1-/- cells are lower than in Hmgn1+/+ cells. Induced expression of wild-type HMGN1, but not of a mutant that does not bind to chromatin, in Hmgn1-/- cells elevates the levels of H3K14ac. In vivo, HMGN1 elevates the levels of H3K14ac by enhancing the action of HAT. In vitro, HMGN1 enhances the ability of PCAF to acetylate nucleosomal, but not free, H3. Thus, HMGN1 modulates the levels of H3K14ac by binding to chromatin. We suggest that HMGN1, and perhaps similar architectural proteins, modulates the levels of acetylation in chromatin by altering the equilibrium generated by the opposing enzymatic activities that continuously modify and de-modify the histone tails in nucleosomes.
authors.affiliation: Protein Section, Laboratory of Metabolism, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
authors.forename: Jae-Hwan
authors.initials: JH
authors.lastname: Lim
authors.forename: Katherine L
authors.initials: KL
authors.lastname: West
authors.forename: Yaffa
authors.initials: Y
authors.lastname: Rubinstein
authors.forename: Michael
authors.initials: M
authors.lastname: Bergel
authors.forename: Yuri V
authors.initials: YV
authors.lastname: Postnikov
authors.forename: Michael
authors.initials: M
authors.lastname: Bustin
mesh_terms: D000107:Acetylation; D000123:Acetyltransferases / Q000378:metabolism; D000818:Animals; D000841:Anisomycin / Q000494:pharmacology; D018797:Cell Cycle Proteins / Q000378:metabolism; D002478:Cells, Cultured; D002843:Chromatin / Q000378:metabolism*; D005347:Fibroblasts; D005786:Gene Expression Regulation; D024241:HMGN1 Protein / Q000235:genetics / Q000378:metabolism*; D051548:Histone Acetyltransferases; D006657:Histones / Q000378:metabolism*; D008239:Lysine / Q000378:metabolism*; D051379:Mice; D009154:Mutation; D009707:Nucleosomes / Q000378:metabolism; D011500:Protein Synthesis Inhibitors / Q000494:pharmacology; D014157:Transcription Factors / Q000378:metabolism; D050880:p300-CBP Transcription Factors; D000099224:p300-CBP-Associated Factor
chemical_list: D000123:Acetyltransferases; D000841:Anisomycin; D018797:Cell Cycle Proteins; D002843:Chromatin; D024241:HMGN1 Protein; D051548:Histone Acetyltransferases; D006657:Histones; D008239:Lysine; D009707:Nucleosomes; D011500:Protein Synthesis Inhibitors; D014157:Transcription Factors; D050880:p300-CBP Transcription Factors; D000099224:p300-CBP-Associated Factor