Chromosomal Protein HMGN1 Modulates Histone H3 Phosphorylation
Here we demonstrate that HMGN1, a nuclear protein that binds to nucleosomes and reduces the compaction of the chromatin fiber, modulates histone posttranslational modifications. In Hmgn1−/− cells, loss of HMGN1 elevates the steady-state levels of phospho-S10-H3 and enhances the rate of stress-induce...
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| Veröffentlicht in: | Molecular cell 2004-08, Vol.15 (4), p.573-584 |
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| creator | Lim, Jae-Hwan Catez, Frédéric Birger, Yehudit West, Katherine L. Prymakowska-Bosak, Marta Postnikov, Yuri V. Bustin, Michael |
| description | Here we demonstrate that HMGN1, a nuclear protein that binds to nucleosomes and reduces the compaction of the chromatin fiber, modulates histone posttranslational modifications. In Hmgn1−/− cells, loss of HMGN1 elevates the steady-state levels of phospho-S10-H3 and enhances the rate of stress-induced phosphorylation of S10-H3. In vitro, HMGN1 reduces the rate of phospho-S10-H3 by hindering the ability of kinases to modify nucleosomal, but not free, H3. During anisomycin treatment, the phosphorylation of HMGN1 precedes that of H3 and leads to a transient weakening of the binding of HMGN1 to chromatin. We propose that the reduced binding of HMGN1 to nucleosomes, or the absence of the protein, improves access of anisomysin-induced kinases to H3. Thus, the levels of posttranslational modifications in chromatin are modulated by nucleosome binding proteins that alter the ability of enzymatic complexes to access and modify their nucleosomal targets. |
| doi_str_mv | 10.1016/j.molcel.2004.08.006 |
| format | Article |
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In Hmgn1−/− cells, loss of HMGN1 elevates the steady-state levels of phospho-S10-H3 and enhances the rate of stress-induced phosphorylation of S10-H3. In vitro, HMGN1 reduces the rate of phospho-S10-H3 by hindering the ability of kinases to modify nucleosomal, but not free, H3. During anisomycin treatment, the phosphorylation of HMGN1 precedes that of H3 and leads to a transient weakening of the binding of HMGN1 to chromatin. We propose that the reduced binding of HMGN1 to nucleosomes, or the absence of the protein, improves access of anisomysin-induced kinases to H3. Thus, the levels of posttranslational modifications in chromatin are modulated by nucleosome binding proteins that alter the ability of enzymatic complexes to access and modify their nucleosomal targets.</description><identifier>ISSN: 1097-2765</identifier><identifier>EISSN: 1097-4164</identifier><identifier>DOI: 10.1016/j.molcel.2004.08.006</identifier><identifier>PMID: 15327773</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Anisomycin - pharmacology ; Cells, Cultured ; Chromatin - metabolism ; Fibroblasts - cytology ; Fibroblasts - drug effects ; Fibroblasts - physiology ; Gene Expression Regulation ; Genes, Immediate-Early ; Histones - metabolism ; HMGN1 Protein - genetics ; HMGN1 Protein - metabolism ; Mice ; Mice, Knockout ; Nucleosomes - metabolism ; Phosphorylation ; Protein Binding ; Protein Processing, Post-Translational ; Protein Synthesis Inhibitors - pharmacology</subject><ispartof>Molecular cell, 2004-08, Vol.15 (4), p.573-584</ispartof><rights>2004 Cell Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c501t-39c7296b509bcf6b7990d6e8f2a06a3433f37ffd0a89f6557c9746720deb55d83</citedby><cites>FETCH-LOGICAL-c501t-39c7296b509bcf6b7990d6e8f2a06a3433f37ffd0a89f6557c9746720deb55d83</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.2004.08.006$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15327773$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lim, Jae-Hwan</creatorcontrib><creatorcontrib>Catez, Frédéric</creatorcontrib><creatorcontrib>Birger, Yehudit</creatorcontrib><creatorcontrib>West, Katherine L.</creatorcontrib><creatorcontrib>Prymakowska-Bosak, Marta</creatorcontrib><creatorcontrib>Postnikov, Yuri V.</creatorcontrib><creatorcontrib>Bustin, Michael</creatorcontrib><title>Chromosomal Protein HMGN1 Modulates Histone H3 Phosphorylation</title><title>Molecular cell</title><addtitle>Mol Cell</addtitle><description>Here we demonstrate that HMGN1, a nuclear protein that binds to nucleosomes and reduces the compaction of the chromatin fiber, modulates histone posttranslational modifications. In Hmgn1−/− cells, loss of HMGN1 elevates the steady-state levels of phospho-S10-H3 and enhances the rate of stress-induced phosphorylation of S10-H3. In vitro, HMGN1 reduces the rate of phospho-S10-H3 by hindering the ability of kinases to modify nucleosomal, but not free, H3. During anisomycin treatment, the phosphorylation of HMGN1 precedes that of H3 and leads to a transient weakening of the binding of HMGN1 to chromatin. We propose that the reduced binding of HMGN1 to nucleosomes, or the absence of the protein, improves access of anisomysin-induced kinases to H3. Thus, the levels of posttranslational modifications in chromatin are modulated by nucleosome binding proteins that alter the ability of enzymatic complexes to access and modify their nucleosomal targets.</description><subject>Animals</subject><subject>Anisomycin - pharmacology</subject><subject>Cells, Cultured</subject><subject>Chromatin - metabolism</subject><subject>Fibroblasts - cytology</subject><subject>Fibroblasts - drug effects</subject><subject>Fibroblasts - physiology</subject><subject>Gene Expression Regulation</subject><subject>Genes, Immediate-Early</subject><subject>Histones - metabolism</subject><subject>HMGN1 Protein - genetics</subject><subject>HMGN1 Protein - metabolism</subject><subject>Mice</subject><subject>Mice, Knockout</subject><subject>Nucleosomes - metabolism</subject><subject>Phosphorylation</subject><subject>Protein Binding</subject><subject>Protein Processing, Post-Translational</subject><subject>Protein Synthesis Inhibitors - pharmacology</subject><issn>1097-2765</issn><issn>1097-4164</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1Lw0AQhhdRrFb_gUhO3hpns9mvS0GKtkKrPeh5STYbuiXJ1t1E6L83JQFvepqBed4Z5kHoDkOMAbPHfVy7SpsqTgDSGEQMwM7QFQbJZylm6fnYJ5zRCboOYQ-AUyrkJZpgShLOOblC88XOu9oFV2dVtPWuNbaJVpvlG442ruiqrDUhWtnQusZEKxJtdy4cds4f-4l1zQ26KLMqmNuxTtHny_PHYjVbvy9fF0_rmaaA2xmRmieS5RRkrkuWcymhYEaUSQYsIykhJeFlWUAmZMko5VrylPEECpNTWggyRQ_D3oN3X50Jrapt6J-vssa4LijGBOZM0H9BLCAlXMgeTAdQexeCN6U6eFtn_qgwqJNgtVeDYHUSrECoXnAfux_3d3ltit_QaLQH5gNgeh3f1ngVtDWNNoX1RreqcPbvCz90QozC</recordid><startdate>20040827</startdate><enddate>20040827</enddate><creator>Lim, Jae-Hwan</creator><creator>Catez, Frédéric</creator><creator>Birger, Yehudit</creator><creator>West, Katherine L.</creator><creator>Prymakowska-Bosak, Marta</creator><creator>Postnikov, Yuri V.</creator><creator>Bustin, Michael</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20040827</creationdate><title>Chromosomal Protein HMGN1 Modulates Histone H3 Phosphorylation</title><author>Lim, Jae-Hwan ; Catez, Frédéric ; Birger, Yehudit ; West, Katherine L. ; Prymakowska-Bosak, Marta ; Postnikov, Yuri V. ; Bustin, Michael</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c501t-39c7296b509bcf6b7990d6e8f2a06a3433f37ffd0a89f6557c9746720deb55d83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Animals</topic><topic>Anisomycin - pharmacology</topic><topic>Cells, Cultured</topic><topic>Chromatin - metabolism</topic><topic>Fibroblasts - cytology</topic><topic>Fibroblasts - drug effects</topic><topic>Fibroblasts - physiology</topic><topic>Gene Expression Regulation</topic><topic>Genes, Immediate-Early</topic><topic>Histones - metabolism</topic><topic>HMGN1 Protein - genetics</topic><topic>HMGN1 Protein - metabolism</topic><topic>Mice</topic><topic>Mice, Knockout</topic><topic>Nucleosomes - metabolism</topic><topic>Phosphorylation</topic><topic>Protein Binding</topic><topic>Protein Processing, Post-Translational</topic><topic>Protein Synthesis Inhibitors - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lim, Jae-Hwan</creatorcontrib><creatorcontrib>Catez, Frédéric</creatorcontrib><creatorcontrib>Birger, Yehudit</creatorcontrib><creatorcontrib>West, Katherine L.</creatorcontrib><creatorcontrib>Prymakowska-Bosak, Marta</creatorcontrib><creatorcontrib>Postnikov, Yuri V.</creatorcontrib><creatorcontrib>Bustin, Michael</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lim, Jae-Hwan</au><au>Catez, Frédéric</au><au>Birger, Yehudit</au><au>West, Katherine L.</au><au>Prymakowska-Bosak, Marta</au><au>Postnikov, Yuri V.</au><au>Bustin, Michael</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Chromosomal Protein HMGN1 Modulates Histone H3 Phosphorylation</atitle><jtitle>Molecular cell</jtitle><addtitle>Mol Cell</addtitle><date>2004-08-27</date><risdate>2004</risdate><volume>15</volume><issue>4</issue><spage>573</spage><epage>584</epage><pages>573-584</pages><issn>1097-2765</issn><eissn>1097-4164</eissn><abstract>Here we demonstrate that HMGN1, a nuclear protein that binds to nucleosomes and reduces the compaction of the chromatin fiber, modulates histone posttranslational modifications. In Hmgn1−/− cells, loss of HMGN1 elevates the steady-state levels of phospho-S10-H3 and enhances the rate of stress-induced phosphorylation of S10-H3. In vitro, HMGN1 reduces the rate of phospho-S10-H3 by hindering the ability of kinases to modify nucleosomal, but not free, H3. During anisomycin treatment, the phosphorylation of HMGN1 precedes that of H3 and leads to a transient weakening of the binding of HMGN1 to chromatin. We propose that the reduced binding of HMGN1 to nucleosomes, or the absence of the protein, improves access of anisomysin-induced kinases to H3. Thus, the levels of posttranslational modifications in chromatin are modulated by nucleosome binding proteins that alter the ability of enzymatic complexes to access and modify their nucleosomal targets.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>15327773</pmid><doi>10.1016/j.molcel.2004.08.006</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Anisomycin - pharmacology Cells, Cultured Chromatin - metabolism Fibroblasts - cytology Fibroblasts - drug effects Fibroblasts - physiology Gene Expression Regulation Genes, Immediate-Early Histones - metabolism HMGN1 Protein - genetics HMGN1 Protein - metabolism Mice Mice, Knockout Nucleosomes - metabolism Phosphorylation Protein Binding Protein Processing, Post-Translational Protein Synthesis Inhibitors - pharmacology |
| title | Chromosomal Protein HMGN1 Modulates Histone H3 Phosphorylation |
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