Expression, purification and proteomic analysis of recombinant histone H4 acetylated at lysine 16
Many histone covalent modifications have been identified and shown to play key regulatory roles in eukaryotic transcription, DNA damage repair, and replication. In vitro experiments designed to understand the mechanistic role of individual modifications require the availability of substantial quanti...
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| Veröffentlicht in: | Proteomics (Weinheim) 2013-05, Vol.13 (10-11), p.1687-1691 |
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| container_issue | 10-11 |
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| container_title | Proteomics (Weinheim) |
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| creator | Kallappagoudar, Satish Dammer, Eric B. Duong, Duc Minh Seyfried, Nicholas T. Lucchesi, John C. |
| description | Many histone covalent modifications have been identified and shown to play key regulatory roles in eukaryotic transcription, DNA damage repair, and replication. In vitro experiments designed to understand the mechanistic role of individual modifications require the availability of substantial quantities of pure histones, homogeneously modified at specific residues. We have applied the amber stop codon/suppressor tRNA strategy to the production of histone H4 acetylated at lysine 16, a particularly important isoform of this histone. Our success relies on adapting the H4 DNA sequence to the codon preference of E. coli and on preventing the premature decay of the H4 mRNA. These modifications to the original procedure render it easily applicable to the generation of any covalently modified histone H4 isoform. |
| doi_str_mv | 10.1002/pmic.201300025 |
| format | Article |
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In vitro experiments designed to understand the mechanistic role of individual modifications require the availability of substantial quantities of pure histones, homogeneously modified at specific residues. We have applied the amber stop codon/suppressor tRNA strategy to the production of histone H4 acetylated at lysine 16, a particularly important isoform of this histone. Our success relies on adapting the H4 DNA sequence to the codon preference of E. coli and on preventing the premature decay of the H4 mRNA. These modifications to the original procedure render it easily applicable to the generation of any covalently modified histone H4 isoform.</description><identifier>ISSN: 1615-9853</identifier><identifier>EISSN: 1615-9861</identifier><identifier>DOI: 10.1002/pmic.201300025</identifier><identifier>PMID: 23554095</identifier><language>eng</language><publisher>Germany: Blackwell Publishing Ltd</publisher><subject>Acetylation ; Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Codon, Terminator ; Escherichia coli ; Gene expression ; Histone ; Histones - biosynthesis ; Histones - chemistry ; Histones - genetics ; Humans ; Lysine - metabolism ; Molecular Sequence Data ; Nucleosome ; Protein Processing, Post-Translational ; Proteomics ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Tandem Mass Spectrometry ; Technology</subject><ispartof>Proteomics (Weinheim), 2013-05, Vol.13 (10-11), p.1687-1691</ispartof><rights>2013 WILEY‐VCH Verlag GmbH & Co. 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These modifications to the original procedure render it easily applicable to the generation of any covalently modified histone H4 isoform.</description><subject>Acetylation</subject><subject>Amino Acid Sequence</subject><subject>Base Sequence</subject><subject>Cloning, Molecular</subject><subject>Codon, Terminator</subject><subject>Escherichia coli</subject><subject>Gene expression</subject><subject>Histone</subject><subject>Histones - biosynthesis</subject><subject>Histones - chemistry</subject><subject>Histones - genetics</subject><subject>Humans</subject><subject>Lysine - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Nucleosome</subject><subject>Protein Processing, Post-Translational</subject><subject>Proteomics</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Tandem Mass Spectrometry</subject><subject>Technology</subject><issn>1615-9853</issn><issn>1615-9861</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVUUlv3CAYRVWjZmmuOUYce4hTVoMvldpJMhMpXVQ1yhEBxg2tbVxgksy_L6NJrPYCPL63SN8D4ASjc4wQeT8N3p4ThCkqiL8CB7jGvGpkjV_Pb073wWFKvxDCQjbiDdgnlHOGGn4A9OXTFF1KPoxncFpH33mrc0FQjy2cYsgulIiCdL9JPsHQwehsGIwf9ZjhvU85jA6uGNTW5U2vs2uhznDLLv-4fgv2Ot0nd_x8H4Hbq8sfi1V183V5vfh4U3kqG1pJbFhHJBFa0rppkOHWWGGtIUx2sulcy5xhWlMhLSZWcNMaLAV35ew4QfQIfNj5TmszuNa6MUfdqyn6QceNCtqr_yejv1c_w4OiQmDKmmLw7tkghj9rl7IafLKu7_XowjopTGuOOKdIFOrpv1lzyMteC4HtCI--d5t5jpHatqa2ram5NfXt8_VCMEKLrNrJylbd0yzT8beqBRVc3X1Zqou75eLTdyHViv4FK8ebvg</recordid><startdate>201305</startdate><enddate>201305</enddate><creator>Kallappagoudar, Satish</creator><creator>Dammer, Eric B.</creator><creator>Duong, Duc Minh</creator><creator>Seyfried, Nicholas T.</creator><creator>Lucchesi, John C.</creator><general>Blackwell Publishing Ltd</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>201305</creationdate><title>Expression, purification and proteomic analysis of recombinant histone H4 acetylated at lysine 16</title><author>Kallappagoudar, Satish ; Dammer, Eric B. ; Duong, Duc Minh ; Seyfried, Nicholas T. ; Lucchesi, John C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-i3893-81b4f2827a836990b5cbc7ccb248f89fed4eb4aa378c12c75bdb1875eb18f5203</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Acetylation</topic><topic>Amino Acid Sequence</topic><topic>Base Sequence</topic><topic>Cloning, Molecular</topic><topic>Codon, Terminator</topic><topic>Escherichia coli</topic><topic>Gene expression</topic><topic>Histone</topic><topic>Histones - biosynthesis</topic><topic>Histones - chemistry</topic><topic>Histones - genetics</topic><topic>Humans</topic><topic>Lysine - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Nucleosome</topic><topic>Protein Processing, Post-Translational</topic><topic>Proteomics</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Tandem Mass Spectrometry</topic><topic>Technology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kallappagoudar, Satish</creatorcontrib><creatorcontrib>Dammer, Eric B.</creatorcontrib><creatorcontrib>Duong, Duc Minh</creatorcontrib><creatorcontrib>Seyfried, Nicholas T.</creatorcontrib><creatorcontrib>Lucchesi, John C.</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proteomics (Weinheim)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kallappagoudar, Satish</au><au>Dammer, Eric B.</au><au>Duong, Duc Minh</au><au>Seyfried, Nicholas T.</au><au>Lucchesi, John C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Expression, purification and proteomic analysis of recombinant histone H4 acetylated at lysine 16</atitle><jtitle>Proteomics (Weinheim)</jtitle><addtitle>Proteomics</addtitle><date>2013-05</date><risdate>2013</risdate><volume>13</volume><issue>10-11</issue><spage>1687</spage><epage>1691</epage><pages>1687-1691</pages><issn>1615-9853</issn><eissn>1615-9861</eissn><abstract>Many histone covalent modifications have been identified and shown to play key regulatory roles in eukaryotic transcription, DNA damage repair, and replication. 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| ispartof | Proteomics (Weinheim), 2013-05, Vol.13 (10-11), p.1687-1691 |
| issn | 1615-9853 1615-9861 |
| language | eng |
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| source | Wiley Online Library - AutoHoldings Journals; MEDLINE |
| subjects | Acetylation Amino Acid Sequence Base Sequence Cloning, Molecular Codon, Terminator Escherichia coli Gene expression Histone Histones - biosynthesis Histones - chemistry Histones - genetics Humans Lysine - metabolism Molecular Sequence Data Nucleosome Protein Processing, Post-Translational Proteomics Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Recombinant Proteins - genetics Tandem Mass Spectrometry Technology |
| title | Expression, purification and proteomic analysis of recombinant histone H4 acetylated at lysine 16 |
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