Comprehensive Phosphoprotein Analysis of Linker Histone H1 from Tetrahymena thermophila
Linker histone H1 is highly phosphorylated in normal growing Tetrahymena thermophila but becomes noticeably dephosphorylated in response to certain conditions such as prolonged starvation. Because phosphorylation of H1 has been associated with the regulation of gene expression, DNA repair, and other...
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| Veröffentlicht in: | Molecular & cellular proteomics 2006-09, Vol.5 (9), p.1593-1609 |
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| creator | Garcia, Benjamin A Joshi, Swati Thomas, C Eric Chitta, Raghu K Diaz, Robert L Busby, Scott A Andrews, Philip C Ogorzalek Loo, Rachel R Shabanowitz, Jeffrey Kelleher, Neil L Mizzen, Craig A Allis, C David Hunt, Donald F |
| description | Linker histone H1 is highly phosphorylated in normal growing Tetrahymena thermophila but becomes noticeably dephosphorylated in response to certain conditions such as prolonged starvation. Because phosphorylation
of H1 has been associated with the regulation of gene expression, DNA repair, and other critical processes, we sought to use
mass spectrometry-based approaches to obtain an in depth phosphorylation âsignatureâ for this linker histone. Histone H1 from
both growing and starved Tetrahymena was analyzed by nanoflow reversed-phase HPLC MS/MS following enzymatic digestions, propionic anhydride derivatization, and
phosphopeptide enrichment via IMAC. We confirmed five phosphorylation sites identified previously and detected two novel sites
of phosphorylation and two novel minor sites of acetylation. The sequential order of phosphorylation on H1 was deduced by
using mass spectrometry to define the modified sites on phosphorylated H1 isoforms separated by cation-exchange chromatography.
Relative levels of site-specific phosphorylation on H1 isolated from growing and starved Tetrahymena were obtained using a combination of stable isotopic labeling, IMAC, and tandem mass spectrometry. |
| doi_str_mv | 10.1074/mcp.M600086-MCP200 |
| format | Article |
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of H1 has been associated with the regulation of gene expression, DNA repair, and other critical processes, we sought to use
mass spectrometry-based approaches to obtain an in depth phosphorylation âsignatureâ for this linker histone. Histone H1 from
both growing and starved Tetrahymena was analyzed by nanoflow reversed-phase HPLC MS/MS following enzymatic digestions, propionic anhydride derivatization, and
phosphopeptide enrichment via IMAC. We confirmed five phosphorylation sites identified previously and detected two novel sites
of phosphorylation and two novel minor sites of acetylation. The sequential order of phosphorylation on H1 was deduced by
using mass spectrometry to define the modified sites on phosphorylated H1 isoforms separated by cation-exchange chromatography.
Relative levels of site-specific phosphorylation on H1 isolated from growing and starved Tetrahymena were obtained using a combination of stable isotopic labeling, IMAC, and tandem mass spectrometry.</description><identifier>ISSN: 1535-9476</identifier><identifier>EISSN: 1535-9484</identifier><identifier>DOI: 10.1074/mcp.M600086-MCP200</identifier><identifier>PMID: 16835217</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Animals ; Binding Sites ; Chromatography, High Pressure Liquid ; Gene Expression Regulation ; Histones - metabolism ; Molecular Sequence Data ; Phosphoproteins - metabolism ; Phosphorylation ; Protein Isoforms - chemistry ; Protein Isoforms - metabolism ; Protein Processing, Post-Translational ; Protozoan Proteins - metabolism ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Starvation ; Tetrahymena thermophila ; Tetrahymena thermophila - growth & development ; Tetrahymena thermophila - metabolism</subject><ispartof>Molecular & cellular proteomics, 2006-09, Vol.5 (9), p.1593-1609</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c401t-36a83020f810985e3cd6de6e84799481224dc4bc62f80e89bb38f66293341ec83</citedby><cites>FETCH-LOGICAL-c401t-36a83020f810985e3cd6de6e84799481224dc4bc62f80e89bb38f66293341ec83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,781,785,27929,27930</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16835217$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Garcia, Benjamin A</creatorcontrib><creatorcontrib>Joshi, Swati</creatorcontrib><creatorcontrib>Thomas, C Eric</creatorcontrib><creatorcontrib>Chitta, Raghu K</creatorcontrib><creatorcontrib>Diaz, Robert L</creatorcontrib><creatorcontrib>Busby, Scott A</creatorcontrib><creatorcontrib>Andrews, Philip C</creatorcontrib><creatorcontrib>Ogorzalek Loo, Rachel R</creatorcontrib><creatorcontrib>Shabanowitz, Jeffrey</creatorcontrib><creatorcontrib>Kelleher, Neil L</creatorcontrib><creatorcontrib>Mizzen, Craig A</creatorcontrib><creatorcontrib>Allis, C David</creatorcontrib><creatorcontrib>Hunt, Donald F</creatorcontrib><title>Comprehensive Phosphoprotein Analysis of Linker Histone H1 from Tetrahymena thermophila</title><title>Molecular & cellular proteomics</title><addtitle>Mol Cell Proteomics</addtitle><description>Linker histone H1 is highly phosphorylated in normal growing Tetrahymena thermophila but becomes noticeably dephosphorylated in response to certain conditions such as prolonged starvation. Because phosphorylation
of H1 has been associated with the regulation of gene expression, DNA repair, and other critical processes, we sought to use
mass spectrometry-based approaches to obtain an in depth phosphorylation âsignatureâ for this linker histone. Histone H1 from
both growing and starved Tetrahymena was analyzed by nanoflow reversed-phase HPLC MS/MS following enzymatic digestions, propionic anhydride derivatization, and
phosphopeptide enrichment via IMAC. We confirmed five phosphorylation sites identified previously and detected two novel sites
of phosphorylation and two novel minor sites of acetylation. The sequential order of phosphorylation on H1 was deduced by
using mass spectrometry to define the modified sites on phosphorylated H1 isoforms separated by cation-exchange chromatography.
Relative levels of site-specific phosphorylation on H1 isolated from growing and starved Tetrahymena were obtained using a combination of stable isotopic labeling, IMAC, and tandem mass spectrometry.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Gene Expression Regulation</subject><subject>Histones - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Phosphoproteins - metabolism</subject><subject>Phosphorylation</subject><subject>Protein Isoforms - chemistry</subject><subject>Protein Isoforms - metabolism</subject><subject>Protein Processing, Post-Translational</subject><subject>Protozoan Proteins - metabolism</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><subject>Starvation</subject><subject>Tetrahymena thermophila</subject><subject>Tetrahymena thermophila - growth & development</subject><subject>Tetrahymena thermophila - metabolism</subject><issn>1535-9476</issn><issn>1535-9484</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkD1PwzAQhi0E4vsPMCBPbCn-iB1nRBVQpCIYihitxL1gQxwHOwX135OqFYxMd8Nz7909CF1QMqGkyK-96SePkhCiZPY4fWaE7KFjKrjIylzl-799IY_QSUrvhDBCC3GIjqhUXDBaHKPXafB9BAtdcl-An21IvQ19DAO4Dt90VbtOLuHQ4LnrPiDimUtD6ADPKG5i8HgBQ6zs2kNX4cFC9KG3rq3O0EFTtQnOd_UUvdzdLqazbP50_zC9mWcmJ3TIuKwUH89qFCWlEsDNUi5BgsqLcnyCMpYvTV4byRpFQJV1zVUjJSs5zykYxU_R1TZ3PPlzBWnQ3iUDbVt1EFZJS6UELUXxL0g3kYyIEWRb0MSQUoRG99H5Kq41JXrjXY_e9c673nofhy536avaw_JvZCd6BPAWsO7NfrsIunbBWPBa6FJTMW7_Ac1vigM</recordid><startdate>20060901</startdate><enddate>20060901</enddate><creator>Garcia, Benjamin A</creator><creator>Joshi, Swati</creator><creator>Thomas, C Eric</creator><creator>Chitta, Raghu K</creator><creator>Diaz, Robert L</creator><creator>Busby, Scott A</creator><creator>Andrews, Philip C</creator><creator>Ogorzalek Loo, Rachel R</creator><creator>Shabanowitz, Jeffrey</creator><creator>Kelleher, Neil L</creator><creator>Mizzen, Craig A</creator><creator>Allis, C David</creator><creator>Hunt, Donald F</creator><general>American Society for Biochemistry and Molecular Biology</general><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>M7N</scope><scope>7X8</scope></search><sort><creationdate>20060901</creationdate><title>Comprehensive Phosphoprotein Analysis of Linker Histone H1 from Tetrahymena thermophila</title><author>Garcia, Benjamin A ; Joshi, Swati ; Thomas, C Eric ; Chitta, Raghu K ; Diaz, Robert L ; Busby, Scott A ; Andrews, Philip C ; Ogorzalek Loo, Rachel R ; Shabanowitz, Jeffrey ; Kelleher, Neil L ; Mizzen, Craig A ; Allis, C David ; Hunt, Donald F</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c401t-36a83020f810985e3cd6de6e84799481224dc4bc62f80e89bb38f66293341ec83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Gene Expression Regulation</topic><topic>Histones - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Phosphoproteins - metabolism</topic><topic>Phosphorylation</topic><topic>Protein Isoforms - chemistry</topic><topic>Protein Isoforms - metabolism</topic><topic>Protein Processing, Post-Translational</topic><topic>Protozoan Proteins - metabolism</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><topic>Starvation</topic><topic>Tetrahymena thermophila</topic><topic>Tetrahymena thermophila - growth & development</topic><topic>Tetrahymena thermophila - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Garcia, Benjamin A</creatorcontrib><creatorcontrib>Joshi, Swati</creatorcontrib><creatorcontrib>Thomas, C Eric</creatorcontrib><creatorcontrib>Chitta, Raghu K</creatorcontrib><creatorcontrib>Diaz, Robert L</creatorcontrib><creatorcontrib>Busby, Scott A</creatorcontrib><creatorcontrib>Andrews, Philip C</creatorcontrib><creatorcontrib>Ogorzalek Loo, Rachel R</creatorcontrib><creatorcontrib>Shabanowitz, Jeffrey</creatorcontrib><creatorcontrib>Kelleher, Neil L</creatorcontrib><creatorcontrib>Mizzen, Craig A</creatorcontrib><creatorcontrib>Allis, C David</creatorcontrib><creatorcontrib>Hunt, Donald F</creatorcontrib><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>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular & cellular proteomics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Garcia, Benjamin A</au><au>Joshi, Swati</au><au>Thomas, C Eric</au><au>Chitta, Raghu K</au><au>Diaz, Robert L</au><au>Busby, Scott A</au><au>Andrews, Philip C</au><au>Ogorzalek Loo, Rachel R</au><au>Shabanowitz, Jeffrey</au><au>Kelleher, Neil L</au><au>Mizzen, Craig A</au><au>Allis, C David</au><au>Hunt, Donald F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Comprehensive Phosphoprotein Analysis of Linker Histone H1 from Tetrahymena thermophila</atitle><jtitle>Molecular & cellular proteomics</jtitle><addtitle>Mol Cell Proteomics</addtitle><date>2006-09-01</date><risdate>2006</risdate><volume>5</volume><issue>9</issue><spage>1593</spage><epage>1609</epage><pages>1593-1609</pages><issn>1535-9476</issn><eissn>1535-9484</eissn><abstract>Linker histone H1 is highly phosphorylated in normal growing Tetrahymena thermophila but becomes noticeably dephosphorylated in response to certain conditions such as prolonged starvation. Because phosphorylation
of H1 has been associated with the regulation of gene expression, DNA repair, and other critical processes, we sought to use
mass spectrometry-based approaches to obtain an in depth phosphorylation âsignatureâ for this linker histone. Histone H1 from
both growing and starved Tetrahymena was analyzed by nanoflow reversed-phase HPLC MS/MS following enzymatic digestions, propionic anhydride derivatization, and
phosphopeptide enrichment via IMAC. We confirmed five phosphorylation sites identified previously and detected two novel sites
of phosphorylation and two novel minor sites of acetylation. The sequential order of phosphorylation on H1 was deduced by
using mass spectrometry to define the modified sites on phosphorylated H1 isoforms separated by cation-exchange chromatography.
Relative levels of site-specific phosphorylation on H1 isolated from growing and starved Tetrahymena were obtained using a combination of stable isotopic labeling, IMAC, and tandem mass spectrometry.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>16835217</pmid><doi>10.1074/mcp.M600086-MCP200</doi><tpages>17</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Animals Binding Sites Chromatography, High Pressure Liquid Gene Expression Regulation Histones - metabolism Molecular Sequence Data Phosphoproteins - metabolism Phosphorylation Protein Isoforms - chemistry Protein Isoforms - metabolism Protein Processing, Post-Translational Protozoan Proteins - metabolism Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Starvation Tetrahymena thermophila Tetrahymena thermophila - growth & development Tetrahymena thermophila - metabolism |
| title | Comprehensive Phosphoprotein Analysis of Linker Histone H1 from Tetrahymena thermophila |
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