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A Genetically Encoded Allysine for the Synthesis of Proteins with Site‐Specific Lysine Dimethylation
Using the amber suppression approach, Nϵ‐(4‐azidobenzoxycarbonyl)‐δ,ϵ‐dehydrolysine, an allysine precursor is genetically encoded in E. coli. Its genetic incorporation followed by two sequential biocompatible reactions allows convenient synthesis of proteins with site‐specific lysine dimethylation....
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| Published in: | Angewandte Chemie International Edition 2017-01, Vol.56 (1), p.212-216 |
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| cited_by | cdi_FETCH-LOGICAL-c5332-9e9fae0d06eab86a91e03047ac909c6714f784452d83e030c441a113287a28623 |
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| cites | cdi_FETCH-LOGICAL-c5332-9e9fae0d06eab86a91e03047ac909c6714f784452d83e030c441a113287a28623 |
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| container_title | Angewandte Chemie International Edition |
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| creator | Wang, Zhipeng A. Zeng, Yu Kurra, Yadagiri Wang, Xin Tharp, Jeffery M. Vatansever, Erol C. Hsu, Willie W. Dai, Susie Fang, Xinqiang Liu, Wenshe R. |
| description | Using the amber suppression approach, Nϵ‐(4‐azidobenzoxycarbonyl)‐δ,ϵ‐dehydrolysine, an allysine precursor is genetically encoded in E. coli. Its genetic incorporation followed by two sequential biocompatible reactions allows convenient synthesis of proteins with site‐specific lysine dimethylation. Using this approach, dimethyl‐histone H3 and p53 proteins have been synthesized and used to probe functions of epigenetic enzymes including histone demethylase LSD1 and histone acetyltransferase Tip60. We confirmed that LSD1 is catalytically active toward H3K4me2 and H3K9me2 but inert toward H3K36me2, and methylation at p53 K372 directly activates Tip60 for its catalyzed acetylation at p53 K120.
Expedient protein synthesis: An allysine precursor, Nϵ‐(4‐azidobenzoxycarbonyl)‐δ,ϵ‐dehydrolysine is genetically encoded in E. coli. Its incorporation followed by Staudinger reduction and reductive amination allows the synthesis of proteins with site‐specific lysine dimethylation. |
| doi_str_mv | 10.1002/anie.201609452 |
| format | article |
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Expedient protein synthesis: An allysine precursor, Nϵ‐(4‐azidobenzoxycarbonyl)‐δ,ϵ‐dehydrolysine is genetically encoded in E. coli. Its incorporation followed by Staudinger reduction and reductive amination allows the synthesis of proteins with site‐specific lysine dimethylation.</description><edition>International ed. in English</edition><identifier>ISSN: 1433-7851</identifier><identifier>EISSN: 1521-3773</identifier><identifier>DOI: 10.1002/anie.201609452</identifier><identifier>PMID: 27910233</identifier><identifier>CODEN: ACIEAY</identifier><language>eng</language><publisher>Germany: Wiley Subscription Services, Inc</publisher><subject>2-Aminoadipic Acid - analogs & derivatives ; 2-Aminoadipic Acid - genetics ; Acetylation ; allysine ; amber suppression ; Biocompatibility ; Chemical synthesis ; dimethyllysine ; E coli ; Escherichia coli - genetics ; Genetic Code ; genetic code expansion ; Histone acetyltransferase ; Histone H3 ; Histones - chemistry ; Histones - genetics ; Humans ; Lysine ; Lysine - analogs & derivatives ; Lysine - chemistry ; Lysine - genetics ; lysine dimethylation ; Methylation ; Models, Molecular ; Mutagenesis, Site-Directed - methods ; p53 Protein ; Protein Processing, Post-Translational ; Proteins ; Tumor Suppressor Protein p53 - chemistry ; Tumor Suppressor Protein p53 - genetics</subject><ispartof>Angewandte Chemie International Edition, 2017-01, Vol.56 (1), p.212-216</ispartof><rights>2017 Wiley‐VCH Verlag GmbH & Co. KGaA, Weinheim</rights><rights>2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.</rights><rights>2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5332-9e9fae0d06eab86a91e03047ac909c6714f784452d83e030c441a113287a28623</citedby><cites>FETCH-LOGICAL-c5332-9e9fae0d06eab86a91e03047ac909c6714f784452d83e030c441a113287a28623</cites><orcidid>0000-0002-7078-6534</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27910233$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Zhipeng A.</creatorcontrib><creatorcontrib>Zeng, Yu</creatorcontrib><creatorcontrib>Kurra, Yadagiri</creatorcontrib><creatorcontrib>Wang, Xin</creatorcontrib><creatorcontrib>Tharp, Jeffery M.</creatorcontrib><creatorcontrib>Vatansever, Erol C.</creatorcontrib><creatorcontrib>Hsu, Willie W.</creatorcontrib><creatorcontrib>Dai, Susie</creatorcontrib><creatorcontrib>Fang, Xinqiang</creatorcontrib><creatorcontrib>Liu, Wenshe R.</creatorcontrib><title>A Genetically Encoded Allysine for the Synthesis of Proteins with Site‐Specific Lysine Dimethylation</title><title>Angewandte Chemie International Edition</title><addtitle>Angew Chem Int Ed Engl</addtitle><description>Using the amber suppression approach, Nϵ‐(4‐azidobenzoxycarbonyl)‐δ,ϵ‐dehydrolysine, an allysine precursor is genetically encoded in E. coli. Its genetic incorporation followed by two sequential biocompatible reactions allows convenient synthesis of proteins with site‐specific lysine dimethylation. Using this approach, dimethyl‐histone H3 and p53 proteins have been synthesized and used to probe functions of epigenetic enzymes including histone demethylase LSD1 and histone acetyltransferase Tip60. We confirmed that LSD1 is catalytically active toward H3K4me2 and H3K9me2 but inert toward H3K36me2, and methylation at p53 K372 directly activates Tip60 for its catalyzed acetylation at p53 K120.
Expedient protein synthesis: An allysine precursor, Nϵ‐(4‐azidobenzoxycarbonyl)‐δ,ϵ‐dehydrolysine is genetically encoded in E. coli. Its incorporation followed by Staudinger reduction and reductive amination allows the synthesis of proteins with site‐specific lysine dimethylation.</description><subject>2-Aminoadipic Acid - analogs & derivatives</subject><subject>2-Aminoadipic Acid - genetics</subject><subject>Acetylation</subject><subject>allysine</subject><subject>amber suppression</subject><subject>Biocompatibility</subject><subject>Chemical synthesis</subject><subject>dimethyllysine</subject><subject>E coli</subject><subject>Escherichia coli - genetics</subject><subject>Genetic Code</subject><subject>genetic code expansion</subject><subject>Histone acetyltransferase</subject><subject>Histone H3</subject><subject>Histones - chemistry</subject><subject>Histones - genetics</subject><subject>Humans</subject><subject>Lysine</subject><subject>Lysine - analogs & derivatives</subject><subject>Lysine - chemistry</subject><subject>Lysine - genetics</subject><subject>lysine dimethylation</subject><subject>Methylation</subject><subject>Models, Molecular</subject><subject>Mutagenesis, Site-Directed - methods</subject><subject>p53 Protein</subject><subject>Protein Processing, Post-Translational</subject><subject>Proteins</subject><subject>Tumor Suppressor Protein p53 - chemistry</subject><subject>Tumor Suppressor Protein p53 - genetics</subject><issn>1433-7851</issn><issn>1521-3773</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><recordid>eNqFkU1vEzEQhi0EoqVw5YgsceGywR_rrwtSVEKpFAFS4Gy53lniamOHtdNqb_wEfiO_BEcp4eMAp5nRPPNqXr0IPaVkRglhL10MMGOESmJawe6hUyoYbbhS_H7tW84bpQU9QY9yvq681kQ-RCdMGUoY56eon-MLiFCCd8Mw4UX0qYMOz-uQQwTcpxGXNeDVFGvJIePU4w9jKhBixrehrPEqFPj-9dtqCz70wePl4fJ12EBZT4MrIcXH6EHvhgxP7uoZ-vRm8fH8bbN8f3F5Pl82XnDOGgOmd0A6IsFdaekMBcJJq5w3xHipaNsr3Vajneb7jW9b6ijlTCvHtGT8DL066G53VxvoPMQyusFux7Bx42STC_bPTQxr-zndWMGI1IZXgRd3AmP6soNc7CZkD8PgIqRdtlS3QlNFmKjo87_Q67QbY7VnGWHSUKMY-xdFteBMSSZIpWYHyo8p5xH648uU2H3Qdh-0PQZdD579bvSI_0y2AuYA3IYBpv_I2fm7y8Uv8R_kSbUL</recordid><startdate>20170102</startdate><enddate>20170102</enddate><creator>Wang, Zhipeng A.</creator><creator>Zeng, Yu</creator><creator>Kurra, Yadagiri</creator><creator>Wang, Xin</creator><creator>Tharp, Jeffery M.</creator><creator>Vatansever, Erol C.</creator><creator>Hsu, Willie W.</creator><creator>Dai, Susie</creator><creator>Fang, Xinqiang</creator><creator>Liu, Wenshe R.</creator><general>Wiley Subscription Services, Inc</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>K9.</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-7078-6534</orcidid></search><sort><creationdate>20170102</creationdate><title>A Genetically Encoded Allysine for the Synthesis of Proteins with Site‐Specific Lysine Dimethylation</title><author>Wang, Zhipeng A. ; Zeng, Yu ; Kurra, Yadagiri ; Wang, Xin ; Tharp, Jeffery M. ; Vatansever, Erol C. ; Hsu, Willie W. ; Dai, Susie ; Fang, Xinqiang ; Liu, Wenshe R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5332-9e9fae0d06eab86a91e03047ac909c6714f784452d83e030c441a113287a28623</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>2-Aminoadipic Acid - analogs & derivatives</topic><topic>2-Aminoadipic Acid - genetics</topic><topic>Acetylation</topic><topic>allysine</topic><topic>amber suppression</topic><topic>Biocompatibility</topic><topic>Chemical synthesis</topic><topic>dimethyllysine</topic><topic>E coli</topic><topic>Escherichia coli - genetics</topic><topic>Genetic Code</topic><topic>genetic code expansion</topic><topic>Histone acetyltransferase</topic><topic>Histone H3</topic><topic>Histones - chemistry</topic><topic>Histones - genetics</topic><topic>Humans</topic><topic>Lysine</topic><topic>Lysine - analogs & derivatives</topic><topic>Lysine - chemistry</topic><topic>Lysine - genetics</topic><topic>lysine dimethylation</topic><topic>Methylation</topic><topic>Models, Molecular</topic><topic>Mutagenesis, Site-Directed - methods</topic><topic>p53 Protein</topic><topic>Protein Processing, Post-Translational</topic><topic>Proteins</topic><topic>Tumor Suppressor Protein p53 - chemistry</topic><topic>Tumor Suppressor Protein p53 - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Zhipeng A.</creatorcontrib><creatorcontrib>Zeng, Yu</creatorcontrib><creatorcontrib>Kurra, Yadagiri</creatorcontrib><creatorcontrib>Wang, Xin</creatorcontrib><creatorcontrib>Tharp, Jeffery M.</creatorcontrib><creatorcontrib>Vatansever, Erol C.</creatorcontrib><creatorcontrib>Hsu, Willie W.</creatorcontrib><creatorcontrib>Dai, Susie</creatorcontrib><creatorcontrib>Fang, Xinqiang</creatorcontrib><creatorcontrib>Liu, Wenshe R.</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>ProQuest Health & Medical Complete (Alumni)</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Angewandte Chemie International Edition</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Zhipeng A.</au><au>Zeng, Yu</au><au>Kurra, Yadagiri</au><au>Wang, Xin</au><au>Tharp, Jeffery M.</au><au>Vatansever, Erol C.</au><au>Hsu, Willie W.</au><au>Dai, Susie</au><au>Fang, Xinqiang</au><au>Liu, Wenshe R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Genetically Encoded Allysine for the Synthesis of Proteins with Site‐Specific Lysine Dimethylation</atitle><jtitle>Angewandte Chemie International Edition</jtitle><addtitle>Angew Chem Int Ed Engl</addtitle><date>2017-01-02</date><risdate>2017</risdate><volume>56</volume><issue>1</issue><spage>212</spage><epage>216</epage><pages>212-216</pages><issn>1433-7851</issn><eissn>1521-3773</eissn><coden>ACIEAY</coden><abstract>Using the amber suppression approach, Nϵ‐(4‐azidobenzoxycarbonyl)‐δ,ϵ‐dehydrolysine, an allysine precursor is genetically encoded in E. coli. Its genetic incorporation followed by two sequential biocompatible reactions allows convenient synthesis of proteins with site‐specific lysine dimethylation. Using this approach, dimethyl‐histone H3 and p53 proteins have been synthesized and used to probe functions of epigenetic enzymes including histone demethylase LSD1 and histone acetyltransferase Tip60. We confirmed that LSD1 is catalytically active toward H3K4me2 and H3K9me2 but inert toward H3K36me2, and methylation at p53 K372 directly activates Tip60 for its catalyzed acetylation at p53 K120.
Expedient protein synthesis: An allysine precursor, Nϵ‐(4‐azidobenzoxycarbonyl)‐δ,ϵ‐dehydrolysine is genetically encoded in E. coli. Its incorporation followed by Staudinger reduction and reductive amination allows the synthesis of proteins with site‐specific lysine dimethylation.</abstract><cop>Germany</cop><pub>Wiley Subscription Services, Inc</pub><pmid>27910233</pmid><doi>10.1002/anie.201609452</doi><tpages>5</tpages><edition>International ed. in English</edition><orcidid>https://orcid.org/0000-0002-7078-6534</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | 2-Aminoadipic Acid - analogs & derivatives 2-Aminoadipic Acid - genetics Acetylation allysine amber suppression Biocompatibility Chemical synthesis dimethyllysine E coli Escherichia coli - genetics Genetic Code genetic code expansion Histone acetyltransferase Histone H3 Histones - chemistry Histones - genetics Humans Lysine Lysine - analogs & derivatives Lysine - chemistry Lysine - genetics lysine dimethylation Methylation Models, Molecular Mutagenesis, Site-Directed - methods p53 Protein Protein Processing, Post-Translational Proteins Tumor Suppressor Protein p53 - chemistry Tumor Suppressor Protein p53 - genetics |
| title | A Genetically Encoded Allysine for the Synthesis of Proteins with Site‐Specific Lysine Dimethylation |
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