Histone H4-K16 acetylation controls chromatin structure and protein interactions
| dc.contributor.author | Shogren-Knaak, Michael | |
| dc.contributor.author | Ishii, Haruhiko | |
| dc.contributor.author | Sun, Jian-Min | |
| dc.contributor.author | Pazin, Michael J. | |
| dc.contributor.author | Davie, James R. | |
| dc.contributor.author | Peterson, Craig L. | |
| dc.date | 2022-08-11T08:09:35.000 | |
| dc.date.accessioned | 2022-08-23T16:36:26Z | |
| dc.date.available | 2022-08-23T16:36:26Z | |
| dc.date.issued | 2006-02-14 | |
| dc.date.submitted | 2009-03-31 | |
| dc.identifier.citation | Science. 2006 Feb 10;311(5762):844-7. <a href="http://dx.doi.org/10.1126/science.1124000">Link to article on publisher's site</a> | |
| dc.identifier.issn | 1095-9203 (Electronic) | |
| dc.identifier.doi | 10.1126/science.1124000 | |
| dc.identifier.pmid | 16469925 | |
| dc.identifier.uri | http://hdl.handle.net/20.500.14038/38787 | |
| dc.description.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. | |
| dc.language.iso | en_US | |
| dc.relation | <a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=16469925&dopt=Abstract">Link to Article in PubMed</a> | |
| dc.relation.url | http://dx.doi.org/10.1126/science.1124000 | |
| dc.subject | Acetylation | |
| dc.subject | Adenosine Triphosphate | |
| dc.subject | Chromatin | |
| dc.subject | *Chromatin Assembly and Disassembly | |
| dc.subject | DNA | |
| dc.subject | Drosophila Proteins | |
| dc.subject | Electrophoresis, Polyacrylamide Gel | |
| dc.subject | Electrophoretic Mobility Shift Assay | |
| dc.subject | Hela Cells | |
| dc.subject | Histones | |
| dc.subject | Humans | |
| dc.subject | Lysine | |
| dc.subject | Magnesium Chloride | |
| dc.subject | Nucleosomes | |
| dc.subject | Protein Conformation | |
| dc.subject | Protein Folding | |
| dc.subject | Protein Processing, Post-Translational | |
| dc.subject | Recombinant Proteins | |
| dc.subject | Transcription Factors | |
| dc.subject | Life Sciences | |
| dc.subject | Medicine and Health Sciences | |
| dc.title | Histone H4-K16 acetylation controls chromatin structure and protein interactions | |
| dc.type | Journal Article | |
| dc.source.journaltitle | Science (New York, N.Y.) | |
| dc.source.volume | 311 | |
| dc.source.issue | 5762 | |
| dc.identifier.legacycoverpage | https://escholarship.umassmed.edu/oapubs/1632 | |
| dc.identifier.contextkey | 805453 | |
| html.description.abstract | <p>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.</p> | |
| dc.identifier.submissionpath | oapubs/1632 | |
| dc.contributor.department | Program in Molecular Medicine | |
| dc.source.pages | 844-7 |
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