Probing the Binding Interfaces of Histone-Aptamer by Photo Cross-Linking Mass Spectrometry
Histone proteins, which could interact with DNA, play important roles in the regulation of chromatin structures, transcription, and other DNA-based biological processes. Here, we developed a novel aptamer-based probe for the analysis of histone H4-aptamer interfaces. This probe contains a DNA sequen...
Gespeichert in:
| Veröffentlicht in: | ACS chemical biology 2017-01, Vol.12 (1), p.57-62 |
|---|---|
| Hauptverfasser: | , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 62 |
|---|---|
| container_issue | 1 |
| container_start_page | 57 |
| container_title | ACS chemical biology |
| container_volume | 12 |
| creator | Lu, Congcong Tian, Shanshan Zhai, Guijin Yuan, Zuofei Li, Yijun He, Xiwen Zhang, Yukui Zhang, Kai |
| description | Histone proteins, which could interact with DNA, play important roles in the regulation of chromatin structures, transcription, and other DNA-based biological processes. Here, we developed a novel aptamer-based probe for the analysis of histone H4-aptamer interfaces. This probe contains a DNA sequence for specific recognition of histone H4, a biotin tag for affinity enrichment, an aryl azide photoactive group for cross-linking and a cleavable disulfide group to dissociate aptamer from labeled histones. We successfully achieved specific enrichment of histone H4 and further developed a new analysis strategy for histone-aptamer interaction by photo cross-linking mass spectrometry. The binding area of histone H4 to aptamer was investigated and discussed for the first time. This strategy exhibits great potential and might further contribute to the understanding of histone–DNA interaction patterns. |
| doi_str_mv | 10.1021/acschembio.6b00797 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1852659554</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1852659554</sourcerecordid><originalsourceid>FETCH-LOGICAL-a408t-2485fc1cf1c18038af9a23b25f636cf9facf7c9b6059c4edf1172e86e8eac2e73</originalsourceid><addsrcrecordid>eNp9kDFPwzAUhC0EoqXwBxiQR5YU20kceywV0EpFVAIWlshxn2lKEwfbGfrvSdRSNqZ3w93p3ofQNSVjShi9U9rrNVRFace8ICST2Qka0jRNIiHj7PSomRygC-83hCQxF_IcDVgmY55yOUQfS2eLsv7EYQ34vqxXvZ7XAZxRGjy2Bs9KH2wN0aQJqgKHix1erm2weOqs99GirL_60LPyHr82oIOzFQS3u0RnRm09XB3uCL0_PrxNZ9Hi5Wk-nSwilRARIpaI1GiqDdVUkFgoIxWLC5YaHnNtZLfDZFoWnKRSJ7AylGYMBAcBSjPI4hG63fc2zn634ENelV7DdqtqsK3PqUgZT2XHorOyvVX30x2YvHFlpdwupyTvmeZ_TPMD0y50c-hviwpWx8gvxM4w3hu6cL6xrau7d_9r_AHviYYL</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1852659554</pqid></control><display><type>article</type><title>Probing the Binding Interfaces of Histone-Aptamer by Photo Cross-Linking Mass Spectrometry</title><source>ACS Publications</source><source>MEDLINE</source><creator>Lu, Congcong ; Tian, Shanshan ; Zhai, Guijin ; Yuan, Zuofei ; Li, Yijun ; He, Xiwen ; Zhang, Yukui ; Zhang, Kai</creator><creatorcontrib>Lu, Congcong ; Tian, Shanshan ; Zhai, Guijin ; Yuan, Zuofei ; Li, Yijun ; He, Xiwen ; Zhang, Yukui ; Zhang, Kai</creatorcontrib><description>Histone proteins, which could interact with DNA, play important roles in the regulation of chromatin structures, transcription, and other DNA-based biological processes. Here, we developed a novel aptamer-based probe for the analysis of histone H4-aptamer interfaces. This probe contains a DNA sequence for specific recognition of histone H4, a biotin tag for affinity enrichment, an aryl azide photoactive group for cross-linking and a cleavable disulfide group to dissociate aptamer from labeled histones. We successfully achieved specific enrichment of histone H4 and further developed a new analysis strategy for histone-aptamer interaction by photo cross-linking mass spectrometry. The binding area of histone H4 to aptamer was investigated and discussed for the first time. This strategy exhibits great potential and might further contribute to the understanding of histone–DNA interaction patterns.</description><identifier>ISSN: 1554-8929</identifier><identifier>EISSN: 1554-8937</identifier><identifier>DOI: 10.1021/acschembio.6b00797</identifier><identifier>PMID: 27936569</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Aptamers, Nucleotide - chemistry ; Aptamers, Nucleotide - metabolism ; Binding Sites ; Biotinylation ; Cross-Linking Reagents - chemistry ; Cross-Linking Reagents - metabolism ; Disulfides - chemistry ; Disulfides - metabolism ; Histones - chemistry ; Histones - metabolism ; Humans ; Light ; Mass Spectrometry</subject><ispartof>ACS chemical biology, 2017-01, Vol.12 (1), p.57-62</ispartof><rights>Copyright © 2016 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a408t-2485fc1cf1c18038af9a23b25f636cf9facf7c9b6059c4edf1172e86e8eac2e73</citedby><cites>FETCH-LOGICAL-a408t-2485fc1cf1c18038af9a23b25f636cf9facf7c9b6059c4edf1172e86e8eac2e73</cites><orcidid>0000-0003-2800-0531</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/acschembio.6b00797$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/acschembio.6b00797$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2751,27054,27902,27903,56715,56765</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27936569$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lu, Congcong</creatorcontrib><creatorcontrib>Tian, Shanshan</creatorcontrib><creatorcontrib>Zhai, Guijin</creatorcontrib><creatorcontrib>Yuan, Zuofei</creatorcontrib><creatorcontrib>Li, Yijun</creatorcontrib><creatorcontrib>He, Xiwen</creatorcontrib><creatorcontrib>Zhang, Yukui</creatorcontrib><creatorcontrib>Zhang, Kai</creatorcontrib><title>Probing the Binding Interfaces of Histone-Aptamer by Photo Cross-Linking Mass Spectrometry</title><title>ACS chemical biology</title><addtitle>ACS Chem. Biol</addtitle><description>Histone proteins, which could interact with DNA, play important roles in the regulation of chromatin structures, transcription, and other DNA-based biological processes. Here, we developed a novel aptamer-based probe for the analysis of histone H4-aptamer interfaces. This probe contains a DNA sequence for specific recognition of histone H4, a biotin tag for affinity enrichment, an aryl azide photoactive group for cross-linking and a cleavable disulfide group to dissociate aptamer from labeled histones. We successfully achieved specific enrichment of histone H4 and further developed a new analysis strategy for histone-aptamer interaction by photo cross-linking mass spectrometry. The binding area of histone H4 to aptamer was investigated and discussed for the first time. This strategy exhibits great potential and might further contribute to the understanding of histone–DNA interaction patterns.</description><subject>Aptamers, Nucleotide - chemistry</subject><subject>Aptamers, Nucleotide - metabolism</subject><subject>Binding Sites</subject><subject>Biotinylation</subject><subject>Cross-Linking Reagents - chemistry</subject><subject>Cross-Linking Reagents - metabolism</subject><subject>Disulfides - chemistry</subject><subject>Disulfides - metabolism</subject><subject>Histones - chemistry</subject><subject>Histones - metabolism</subject><subject>Humans</subject><subject>Light</subject><subject>Mass Spectrometry</subject><issn>1554-8929</issn><issn>1554-8937</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kDFPwzAUhC0EoqXwBxiQR5YU20kceywV0EpFVAIWlshxn2lKEwfbGfrvSdRSNqZ3w93p3ofQNSVjShi9U9rrNVRFace8ICST2Qka0jRNIiHj7PSomRygC-83hCQxF_IcDVgmY55yOUQfS2eLsv7EYQ34vqxXvZ7XAZxRGjy2Bs9KH2wN0aQJqgKHix1erm2weOqs99GirL_60LPyHr82oIOzFQS3u0RnRm09XB3uCL0_PrxNZ9Hi5Wk-nSwilRARIpaI1GiqDdVUkFgoIxWLC5YaHnNtZLfDZFoWnKRSJ7AylGYMBAcBSjPI4hG63fc2zn634ENelV7DdqtqsK3PqUgZT2XHorOyvVX30x2YvHFlpdwupyTvmeZ_TPMD0y50c-hviwpWx8gvxM4w3hu6cL6xrau7d_9r_AHviYYL</recordid><startdate>20170120</startdate><enddate>20170120</enddate><creator>Lu, Congcong</creator><creator>Tian, Shanshan</creator><creator>Zhai, Guijin</creator><creator>Yuan, Zuofei</creator><creator>Li, Yijun</creator><creator>He, Xiwen</creator><creator>Zhang, Yukui</creator><creator>Zhang, Kai</creator><general>American Chemical Society</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>7X8</scope><orcidid>https://orcid.org/0000-0003-2800-0531</orcidid></search><sort><creationdate>20170120</creationdate><title>Probing the Binding Interfaces of Histone-Aptamer by Photo Cross-Linking Mass Spectrometry</title><author>Lu, Congcong ; Tian, Shanshan ; Zhai, Guijin ; Yuan, Zuofei ; Li, Yijun ; He, Xiwen ; Zhang, Yukui ; Zhang, Kai</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a408t-2485fc1cf1c18038af9a23b25f636cf9facf7c9b6059c4edf1172e86e8eac2e73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Aptamers, Nucleotide - chemistry</topic><topic>Aptamers, Nucleotide - metabolism</topic><topic>Binding Sites</topic><topic>Biotinylation</topic><topic>Cross-Linking Reagents - chemistry</topic><topic>Cross-Linking Reagents - metabolism</topic><topic>Disulfides - chemistry</topic><topic>Disulfides - metabolism</topic><topic>Histones - chemistry</topic><topic>Histones - metabolism</topic><topic>Humans</topic><topic>Light</topic><topic>Mass Spectrometry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lu, Congcong</creatorcontrib><creatorcontrib>Tian, Shanshan</creatorcontrib><creatorcontrib>Zhai, Guijin</creatorcontrib><creatorcontrib>Yuan, Zuofei</creatorcontrib><creatorcontrib>Li, Yijun</creatorcontrib><creatorcontrib>He, Xiwen</creatorcontrib><creatorcontrib>Zhang, Yukui</creatorcontrib><creatorcontrib>Zhang, Kai</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>ACS chemical biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lu, Congcong</au><au>Tian, Shanshan</au><au>Zhai, Guijin</au><au>Yuan, Zuofei</au><au>Li, Yijun</au><au>He, Xiwen</au><au>Zhang, Yukui</au><au>Zhang, Kai</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Probing the Binding Interfaces of Histone-Aptamer by Photo Cross-Linking Mass Spectrometry</atitle><jtitle>ACS chemical biology</jtitle><addtitle>ACS Chem. Biol</addtitle><date>2017-01-20</date><risdate>2017</risdate><volume>12</volume><issue>1</issue><spage>57</spage><epage>62</epage><pages>57-62</pages><issn>1554-8929</issn><eissn>1554-8937</eissn><abstract>Histone proteins, which could interact with DNA, play important roles in the regulation of chromatin structures, transcription, and other DNA-based biological processes. Here, we developed a novel aptamer-based probe for the analysis of histone H4-aptamer interfaces. This probe contains a DNA sequence for specific recognition of histone H4, a biotin tag for affinity enrichment, an aryl azide photoactive group for cross-linking and a cleavable disulfide group to dissociate aptamer from labeled histones. We successfully achieved specific enrichment of histone H4 and further developed a new analysis strategy for histone-aptamer interaction by photo cross-linking mass spectrometry. The binding area of histone H4 to aptamer was investigated and discussed for the first time. This strategy exhibits great potential and might further contribute to the understanding of histone–DNA interaction patterns.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>27936569</pmid><doi>10.1021/acschembio.6b00797</doi><tpages>6</tpages><orcidid>https://orcid.org/0000-0003-2800-0531</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1554-8929 |
| ispartof | ACS chemical biology, 2017-01, Vol.12 (1), p.57-62 |
| issn | 1554-8929 1554-8937 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1852659554 |
| source | ACS Publications; MEDLINE |
| subjects | Aptamers, Nucleotide - chemistry Aptamers, Nucleotide - metabolism Binding Sites Biotinylation Cross-Linking Reagents - chemistry Cross-Linking Reagents - metabolism Disulfides - chemistry Disulfides - metabolism Histones - chemistry Histones - metabolism Humans Light Mass Spectrometry |
| title | Probing the Binding Interfaces of Histone-Aptamer by Photo Cross-Linking Mass Spectrometry |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-27T08%3A30%3A34IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Probing%20the%20Binding%20Interfaces%20of%20Histone-Aptamer%20by%20Photo%20Cross-Linking%20Mass%20Spectrometry&rft.jtitle=ACS%20chemical%20biology&rft.au=Lu,%20Congcong&rft.date=2017-01-20&rft.volume=12&rft.issue=1&rft.spage=57&rft.epage=62&rft.pages=57-62&rft.issn=1554-8929&rft.eissn=1554-8937&rft_id=info:doi/10.1021/acschembio.6b00797&rft_dat=%3Cproquest_cross%3E1852659554%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1852659554&rft_id=info:pmid/27936569&rfr_iscdi=true |