Thiirane linkers directed histone H2A diubiquitination suggests plasticity in 53BP1 recognition
Polyubiquitination with diverse linkages on histones provides another layer of accuracy and complexity for epigenetic regulation, which is rarely studied. Herein, K27 or K48-diubiquitin modified H2A analogues were chemically synthesized using thiirane linkers. These permitted in vitro binding studie...
Gespeichert in:
| Veröffentlicht in: | Chemical communications (Cambridge, England) England), 2019-10, Vol.55 (84), p.12639-12642 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 12642 |
|---|---|
| container_issue | 84 |
| container_start_page | 12639 |
| container_title | Chemical communications (Cambridge, England) |
| container_volume | 55 |
| creator | Liang, Jun Gong, Qingyue Li, Ying Zheng, Yong Zheng, Ji-Shen Tian, Changlin Li, Jia-Bin |
| description | Polyubiquitination with diverse linkages on histones provides another layer of accuracy and complexity for epigenetic regulation, which is rarely studied. Herein, K27 or K48-diubiquitin modified H2A analogues were chemically synthesized using thiirane linkers. These permitted
in vitro
binding studies suggested the plasticity of ubiquitin chains in 53BP1 recognition.
Four diubiquitinated H2A analogues were newly synthesized and used to reveal the plasticity of ubiquitin chains in 53BP1 recognition. |
| doi_str_mv | 10.1039/c9cc05526f |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_rsc_p</sourceid><recordid>TN_cdi_proquest_miscellaneous_2300598976</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2300598976</sourcerecordid><originalsourceid>FETCH-LOGICAL-c429t-97b700abd7bec7925d3b2964d7848a99252a5a0015fd98364c9b4de2b43d95d43</originalsourceid><addsrcrecordid>eNp9kc9LwzAUx4MoTqcX70rFiwjVtEna5jiLc8JADxO8hfzqltm1XdIe9t-bujnBg7m88N6HL9_3fQBcRPA-gog-SColJCROigNwEqEEhwRnH4f9n9AwRZgMwKlzS-hfRLJjMEC-QIToCWCzhTGWVzooTfWprQuUsVq2WgUL49raDybxyDc7YdadaU3FW1NXgevmc-1aFzQld62Rpt0EpgoIenyLAi9QzyvTg2fgqOCl0-e7OgTv46dZPgmnr88v-WgaShzTNqSpSCHkQqVCy5TGRCER0wSrNMMZp74Rc8J7-4WimV9RUoGVjgVGihKF0RDcbnUbW68774ytjJO6LP1qdedYjCAkNKNp4tGbP-iy7mzl3fVUAlNIceSpuy0lbe2c1QVrrFlxu2ERZH3sLKd5_h372MNXO8lOrLTaoz85e-B6C1gn99Pfu7FGFZ65_I9BX2YEkck</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2306070941</pqid></control><display><type>article</type><title>Thiirane linkers directed histone H2A diubiquitination suggests plasticity in 53BP1 recognition</title><source>MEDLINE</source><source>Royal Society Of Chemistry Journals 2008-</source><source>Alma/SFX Local Collection</source><creator>Liang, Jun ; Gong, Qingyue ; Li, Ying ; Zheng, Yong ; Zheng, Ji-Shen ; Tian, Changlin ; Li, Jia-Bin</creator><creatorcontrib>Liang, Jun ; Gong, Qingyue ; Li, Ying ; Zheng, Yong ; Zheng, Ji-Shen ; Tian, Changlin ; Li, Jia-Bin</creatorcontrib><description>Polyubiquitination with diverse linkages on histones provides another layer of accuracy and complexity for epigenetic regulation, which is rarely studied. Herein, K27 or K48-diubiquitin modified H2A analogues were chemically synthesized using thiirane linkers. These permitted
in vitro
binding studies suggested the plasticity of ubiquitin chains in 53BP1 recognition.
Four diubiquitinated H2A analogues were newly synthesized and used to reveal the plasticity of ubiquitin chains in 53BP1 recognition.</description><identifier>ISSN: 1359-7345</identifier><identifier>EISSN: 1364-548X</identifier><identifier>DOI: 10.1039/c9cc05526f</identifier><identifier>PMID: 31580339</identifier><language>eng</language><publisher>England: Royal Society of Chemistry</publisher><subject>Histones ; Histones - chemistry ; Organic chemistry ; Plastic properties ; Polyubiquitin - chemistry ; Protein Binding ; Recognition ; Recombinant Proteins - chemistry ; Sulfides - chemistry ; Tumor Suppressor p53-Binding Protein 1 - chemistry ; Ubiquitination</subject><ispartof>Chemical communications (Cambridge, England), 2019-10, Vol.55 (84), p.12639-12642</ispartof><rights>Copyright Royal Society of Chemistry 2019</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c429t-97b700abd7bec7925d3b2964d7848a99252a5a0015fd98364c9b4de2b43d95d43</citedby><cites>FETCH-LOGICAL-c429t-97b700abd7bec7925d3b2964d7848a99252a5a0015fd98364c9b4de2b43d95d43</cites><orcidid>0000-0002-5308-5787 ; 0000-0001-9315-900X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27922,27923</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31580339$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Liang, Jun</creatorcontrib><creatorcontrib>Gong, Qingyue</creatorcontrib><creatorcontrib>Li, Ying</creatorcontrib><creatorcontrib>Zheng, Yong</creatorcontrib><creatorcontrib>Zheng, Ji-Shen</creatorcontrib><creatorcontrib>Tian, Changlin</creatorcontrib><creatorcontrib>Li, Jia-Bin</creatorcontrib><title>Thiirane linkers directed histone H2A diubiquitination suggests plasticity in 53BP1 recognition</title><title>Chemical communications (Cambridge, England)</title><addtitle>Chem Commun (Camb)</addtitle><description>Polyubiquitination with diverse linkages on histones provides another layer of accuracy and complexity for epigenetic regulation, which is rarely studied. Herein, K27 or K48-diubiquitin modified H2A analogues were chemically synthesized using thiirane linkers. These permitted
in vitro
binding studies suggested the plasticity of ubiquitin chains in 53BP1 recognition.
Four diubiquitinated H2A analogues were newly synthesized and used to reveal the plasticity of ubiquitin chains in 53BP1 recognition.</description><subject>Histones</subject><subject>Histones - chemistry</subject><subject>Organic chemistry</subject><subject>Plastic properties</subject><subject>Polyubiquitin - chemistry</subject><subject>Protein Binding</subject><subject>Recognition</subject><subject>Recombinant Proteins - chemistry</subject><subject>Sulfides - chemistry</subject><subject>Tumor Suppressor p53-Binding Protein 1 - chemistry</subject><subject>Ubiquitination</subject><issn>1359-7345</issn><issn>1364-548X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kc9LwzAUx4MoTqcX70rFiwjVtEna5jiLc8JADxO8hfzqltm1XdIe9t-bujnBg7m88N6HL9_3fQBcRPA-gog-SColJCROigNwEqEEhwRnH4f9n9AwRZgMwKlzS-hfRLJjMEC-QIToCWCzhTGWVzooTfWprQuUsVq2WgUL49raDybxyDc7YdadaU3FW1NXgevmc-1aFzQld62Rpt0EpgoIenyLAi9QzyvTg2fgqOCl0-e7OgTv46dZPgmnr88v-WgaShzTNqSpSCHkQqVCy5TGRCER0wSrNMMZp74Rc8J7-4WimV9RUoGVjgVGihKF0RDcbnUbW68774ytjJO6LP1qdedYjCAkNKNp4tGbP-iy7mzl3fVUAlNIceSpuy0lbe2c1QVrrFlxu2ERZH3sLKd5_h372MNXO8lOrLTaoz85e-B6C1gn99Pfu7FGFZ65_I9BX2YEkck</recordid><startdate>20191017</startdate><enddate>20191017</enddate><creator>Liang, Jun</creator><creator>Gong, Qingyue</creator><creator>Li, Ying</creator><creator>Zheng, Yong</creator><creator>Zheng, Ji-Shen</creator><creator>Tian, Changlin</creator><creator>Li, Jia-Bin</creator><general>Royal Society of Chemistry</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>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>L7M</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-5308-5787</orcidid><orcidid>https://orcid.org/0000-0001-9315-900X</orcidid></search><sort><creationdate>20191017</creationdate><title>Thiirane linkers directed histone H2A diubiquitination suggests plasticity in 53BP1 recognition</title><author>Liang, Jun ; Gong, Qingyue ; Li, Ying ; Zheng, Yong ; Zheng, Ji-Shen ; Tian, Changlin ; Li, Jia-Bin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c429t-97b700abd7bec7925d3b2964d7848a99252a5a0015fd98364c9b4de2b43d95d43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Histones</topic><topic>Histones - chemistry</topic><topic>Organic chemistry</topic><topic>Plastic properties</topic><topic>Polyubiquitin - chemistry</topic><topic>Protein Binding</topic><topic>Recognition</topic><topic>Recombinant Proteins - chemistry</topic><topic>Sulfides - chemistry</topic><topic>Tumor Suppressor p53-Binding Protein 1 - chemistry</topic><topic>Ubiquitination</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Liang, Jun</creatorcontrib><creatorcontrib>Gong, Qingyue</creatorcontrib><creatorcontrib>Li, Ying</creatorcontrib><creatorcontrib>Zheng, Yong</creatorcontrib><creatorcontrib>Zheng, Ji-Shen</creatorcontrib><creatorcontrib>Tian, Changlin</creatorcontrib><creatorcontrib>Li, Jia-Bin</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Engineered Materials Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>MEDLINE - Academic</collection><jtitle>Chemical communications (Cambridge, England)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Liang, Jun</au><au>Gong, Qingyue</au><au>Li, Ying</au><au>Zheng, Yong</au><au>Zheng, Ji-Shen</au><au>Tian, Changlin</au><au>Li, Jia-Bin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Thiirane linkers directed histone H2A diubiquitination suggests plasticity in 53BP1 recognition</atitle><jtitle>Chemical communications (Cambridge, England)</jtitle><addtitle>Chem Commun (Camb)</addtitle><date>2019-10-17</date><risdate>2019</risdate><volume>55</volume><issue>84</issue><spage>12639</spage><epage>12642</epage><pages>12639-12642</pages><issn>1359-7345</issn><eissn>1364-548X</eissn><abstract>Polyubiquitination with diverse linkages on histones provides another layer of accuracy and complexity for epigenetic regulation, which is rarely studied. Herein, K27 or K48-diubiquitin modified H2A analogues were chemically synthesized using thiirane linkers. These permitted
in vitro
binding studies suggested the plasticity of ubiquitin chains in 53BP1 recognition.
Four diubiquitinated H2A analogues were newly synthesized and used to reveal the plasticity of ubiquitin chains in 53BP1 recognition.</abstract><cop>England</cop><pub>Royal Society of Chemistry</pub><pmid>31580339</pmid><doi>10.1039/c9cc05526f</doi><tpages>4</tpages><orcidid>https://orcid.org/0000-0002-5308-5787</orcidid><orcidid>https://orcid.org/0000-0001-9315-900X</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1359-7345 |
| ispartof | Chemical communications (Cambridge, England), 2019-10, Vol.55 (84), p.12639-12642 |
| issn | 1359-7345 1364-548X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_2300598976 |
| source | MEDLINE; Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection |
| subjects | Histones Histones - chemistry Organic chemistry Plastic properties Polyubiquitin - chemistry Protein Binding Recognition Recombinant Proteins - chemistry Sulfides - chemistry Tumor Suppressor p53-Binding Protein 1 - chemistry Ubiquitination |
| title | Thiirane linkers directed histone H2A diubiquitination suggests plasticity in 53BP1 recognition |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-14T01%3A22%3A28IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_rsc_p&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Thiirane%20linkers%20directed%20histone%20H2A%20diubiquitination%20suggests%20plasticity%20in%2053BP1%20recognition&rft.jtitle=Chemical%20communications%20(Cambridge,%20England)&rft.au=Liang,%20Jun&rft.date=2019-10-17&rft.volume=55&rft.issue=84&rft.spage=12639&rft.epage=12642&rft.pages=12639-12642&rft.issn=1359-7345&rft.eissn=1364-548X&rft_id=info:doi/10.1039/c9cc05526f&rft_dat=%3Cproquest_rsc_p%3E2300598976%3C/proquest_rsc_p%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2306070941&rft_id=info:pmid/31580339&rfr_iscdi=true |