Title

Histone H4-K16 acetylation controls chromatin structure and protein interactions

UMMS Affiliation

Program in Molecular Medicine

Publication Date

2-14-2006

Document Type

Article

Subjects

Acetylation; Adenosine Triphosphate; Chromatin; *Chromatin Assembly and Disassembly; DNA; Drosophila Proteins; Electrophoresis, Polyacrylamide Gel; Electrophoretic Mobility Shift Assay; Hela Cells; Histones; Humans; Lysine; Magnesium Chloride; Nucleosomes; Protein Conformation; Protein Folding; Protein Processing, Post-Translational; Recombinant Proteins; Transcription Factors

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

Acetylation of histone H4 on lysine 16 (H4-K16Ac) is a prevalent and reversible posttranslational chromatin modification in eukaryotes. To characterize the structural and functional role of this mark, we used a native chemical ligation strategy to generate histone H4 that was homogeneously acetylated at K16. The incorporation of this modified histone into nucleosomal arrays inhibits the formation of compact 30-nanometer-like fibers and impedes the ability of chromatin to form cross-fiber interactions. H4-K16Ac also inhibits the ability of the adenosine triphosphate-utilizing chromatin assembly and remodeling enzyme ACF to mobilize a mononucleosome, indicating that this single histone modification modulates both higher order chromatin structure and functional interactions between a nonhistone protein and the chromatin fiber.

Rights and Permissions

Citation: Science. 2006 Feb 10;311(5762):844-7. Link to article on publisher's site

DOI of Published Version

10.1126/science.1124000

Related Resources

Link to Article in PubMed

Journal/Book/Conference Title

Science (New York, N.Y.)

PubMed ID

16469925