Molecular Basis for the Recognition of Phosphorylated and Phosphoacetylated Histone H3 by 14-3-3
Phosphorylation of histone H3 is implicated in transcriptional activation and chromosome condensation, but its immediate molecular function has remained obscure. By affinity chromatography of nuclear extracts against modified H3 tail peptides, we identified 14-3-3 isoforms as proteins that bind thes...
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| Veröffentlicht in: | Molecular cell 2005-10, Vol.20 (2), p.199-211 |
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| creator | Macdonald, Neil Welburn, Julie P.I. Noble, Martin E.M. Nguyen, Anhco Yaffe, Michael B. Clynes, David Moggs, Jonathan G. Orphanides, George Thomson, Stuart Edmunds, John W. Clayton, Alison L. Endicott, Jane A. Mahadevan, Louis C. |
| description | Phosphorylation of histone H3 is implicated in transcriptional activation and chromosome condensation, but its immediate molecular function has remained obscure. By affinity chromatography of nuclear extracts against modified H3 tail peptides, we identified 14-3-3 isoforms as proteins that bind these tails in a strictly phosphorylation-dependent manner. Acetylation of lysines 9 and 14 does not impede 14-3-3 binding to serine 10-phosphorylated H3 tails. In vivo, 14-3-3 is inducibly recruited to c-
fos and c-
jun nucleosomes upon gene activation, concomitant with H3 phosphoacetylation. We have determined the structures of 14-3-3ζ complexed with serine 10-phosphorylated or phosphoacetylated H3 peptides. These reveal a distinct mode of 14-3-3/phosphopeptide binding and provide a structural understanding for the lack of effect of acetylation at lysines 9 and 14 on this interaction. 14-3-3 isoforms thus represent a class of proteins that mediate the effect of histone phosphorylation at inducible genes. |
| doi_str_mv | 10.1016/j.molcel.2005.08.032 |
| format | Article |
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jun nucleosomes upon gene activation, concomitant with H3 phosphoacetylation. We have determined the structures of 14-3-3ζ complexed with serine 10-phosphorylated or phosphoacetylated H3 peptides. These reveal a distinct mode of 14-3-3/phosphopeptide binding and provide a structural understanding for the lack of effect of acetylation at lysines 9 and 14 on this interaction. 14-3-3 isoforms thus represent a class of proteins that mediate the effect of histone phosphorylation at inducible genes.</description><identifier>ISSN: 1097-2765</identifier><identifier>EISSN: 1097-4164</identifier><identifier>DOI: 10.1016/j.molcel.2005.08.032</identifier><identifier>PMID: 16246723</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>14-3-3 Proteins - chemistry ; 14-3-3 Proteins - metabolism ; Acetylation ; Amino Acid Sequence ; Animals ; Cell Line ; Crystallography, X-Ray ; HeLa Cells ; Histones - chemistry ; Histones - isolation & purification ; Histones - metabolism ; Humans ; Mice ; Models, Molecular ; Molecular Sequence Data ; Nucleosomes - genetics ; Nucleosomes - metabolism ; Phosphorylation ; Protein Conformation ; Protein Structure, Tertiary ; Proto-Oncogene Proteins c-fos - genetics ; Proto-Oncogene Proteins c-fos - metabolism ; Proto-Oncogene Proteins c-jun - genetics ; Proto-Oncogene Proteins c-jun - metabolism ; Sequence Alignment ; Serine - chemistry ; Serine - metabolism</subject><ispartof>Molecular cell, 2005-10, Vol.20 (2), p.199-211</ispartof><rights>2005 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c406t-17e9e4adc82300425503b966dc07c312144a04d263052f16afc5d1dce77d1dc83</citedby><cites>FETCH-LOGICAL-c406t-17e9e4adc82300425503b966dc07c312144a04d263052f16afc5d1dce77d1dc83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.molcel.2005.08.032$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,45974</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16246723$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Macdonald, Neil</creatorcontrib><creatorcontrib>Welburn, Julie P.I.</creatorcontrib><creatorcontrib>Noble, Martin E.M.</creatorcontrib><creatorcontrib>Nguyen, Anhco</creatorcontrib><creatorcontrib>Yaffe, Michael B.</creatorcontrib><creatorcontrib>Clynes, David</creatorcontrib><creatorcontrib>Moggs, Jonathan G.</creatorcontrib><creatorcontrib>Orphanides, George</creatorcontrib><creatorcontrib>Thomson, Stuart</creatorcontrib><creatorcontrib>Edmunds, John W.</creatorcontrib><creatorcontrib>Clayton, Alison L.</creatorcontrib><creatorcontrib>Endicott, Jane A.</creatorcontrib><creatorcontrib>Mahadevan, Louis C.</creatorcontrib><title>Molecular Basis for the Recognition of Phosphorylated and Phosphoacetylated Histone H3 by 14-3-3</title><title>Molecular cell</title><addtitle>Mol Cell</addtitle><description>Phosphorylation of histone H3 is implicated in transcriptional activation and chromosome condensation, but its immediate molecular function has remained obscure. By affinity chromatography of nuclear extracts against modified H3 tail peptides, we identified 14-3-3 isoforms as proteins that bind these tails in a strictly phosphorylation-dependent manner. Acetylation of lysines 9 and 14 does not impede 14-3-3 binding to serine 10-phosphorylated H3 tails. In vivo, 14-3-3 is inducibly recruited to c-
fos and c-
jun nucleosomes upon gene activation, concomitant with H3 phosphoacetylation. We have determined the structures of 14-3-3ζ complexed with serine 10-phosphorylated or phosphoacetylated H3 peptides. 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fos and c-
jun nucleosomes upon gene activation, concomitant with H3 phosphoacetylation. We have determined the structures of 14-3-3ζ complexed with serine 10-phosphorylated or phosphoacetylated H3 peptides. These reveal a distinct mode of 14-3-3/phosphopeptide binding and provide a structural understanding for the lack of effect of acetylation at lysines 9 and 14 on this interaction. 14-3-3 isoforms thus represent a class of proteins that mediate the effect of histone phosphorylation at inducible genes.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>16246723</pmid><doi>10.1016/j.molcel.2005.08.032</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 14-3-3 Proteins - chemistry 14-3-3 Proteins - metabolism Acetylation Amino Acid Sequence Animals Cell Line Crystallography, X-Ray HeLa Cells Histones - chemistry Histones - isolation & purification Histones - metabolism Humans Mice Models, Molecular Molecular Sequence Data Nucleosomes - genetics Nucleosomes - metabolism Phosphorylation Protein Conformation Protein Structure, Tertiary Proto-Oncogene Proteins c-fos - genetics Proto-Oncogene Proteins c-fos - metabolism Proto-Oncogene Proteins c-jun - genetics Proto-Oncogene Proteins c-jun - metabolism Sequence Alignment Serine - chemistry Serine - metabolism |
| title | Molecular Basis for the Recognition of Phosphorylated and Phosphoacetylated Histone H3 by 14-3-3 |
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