A Genetically Encoded FRET Probe to Detect Intranucleosomal Histone H3K9 or H3K14 Acetylation Using BRD4, a BET Family Member
Acetylation is a well-characterized histone modification, which plays important roles in controlling epigenetic gene expression, and its malfunction is tightly associated with cancer. By taking advantage of the specific binding of BRD4 to acetylated lysine residues, we developed a FRET-based probe f...
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| Veröffentlicht in: | ACS chemical biology 2016-03, Vol.11 (3), p.729-733 |
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| creator | Nakaoka, Shiho Sasaki, Kazuki Ito, Akihiro Nakao, Yoichi Yoshida, Minoru |
| description | Acetylation is a well-characterized histone modification, which plays important roles in controlling epigenetic gene expression, and its malfunction is tightly associated with cancer. By taking advantage of the specific binding of BRD4 to acetylated lysine residues, we developed a FRET-based probe for visualizing histone H3 acetylation in living cells. BRD4, a protein known to be involved in acute myeloid leukemia and nuclear protein in testis midline carcinoma, recognizes the acetylation of histone H3 via its bromodomains. The probe exhibited a significant change in FRET signaling that was dependent on histone H3 acetylation. Mutagenesis studies revealed that an increase in the emission ratio reflected the acetylation of either K9 or K14 of histone H3 within the probe. Since BRD4 has increasingly drawn attention as a new anticancer drug target, we demonstrated that the developed fluorescent probe will also serve as a powerful tool to evaluate BRD4 inhibitors in living cells. |
| doi_str_mv | 10.1021/cb501046t |
| format | Article |
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Since BRD4 has increasingly drawn attention as a new anticancer drug target, we demonstrated that the developed fluorescent probe will also serve as a powerful tool to evaluate BRD4 inhibitors in living cells.</description><subject>Acetylation</subject><subject>Animals</subject><subject>Cercopithecus aethiops</subject><subject>COS Cells</subject><subject>Fluorescence Resonance Energy Transfer</subject><subject>Gene Expression Regulation</subject><subject>Histone Deacetylase Inhibitors</subject><subject>Histones - metabolism</subject><subject>Humans</subject><subject>Nuclear Proteins - genetics</subject><subject>Nuclear Proteins - metabolism</subject><subject>Transcription Factors - genetics</subject><subject>Transcription Factors - metabolism</subject><subject>Transgenes</subject><issn>1554-8929</issn><issn>1554-8937</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkD1PwzAURS0EoqUw8AeQFwYkCrZjJ_bY71YUgap2jmzHQakSu7LdoQP_nVSFTkz3DUfnXV0A7jF6wYjgV60Ywoim8QJ0MWO0z0WSXZ5vIjrgJoQtQjRJubgGHcIETQniXfA9gDNjTay0rOsDnFjtClPA6Wqyhp_eKQOjg2MTjY5wYaOXdq9r44JrZA3nVYjOGjhP3gR0_piYwoE28VDLWDkLN6GyX3C4GtNnKOGwlU5lU7WP3k2jjL8FV6Wsg7n7zR7YTCfr0by__JgtRoNlXyYcx36ZKkwx01na1k814yRNMFUZ4oJmGSqLRCiBBCdCldJwxhlOlWQJLigihGdJDzydvNq7ELwp852vGukPOUb5ccL8PGHLPpzY3V41pjiTf5u1wOMJkDrkW7f3tq3-j-gHl3p0HA</recordid><startdate>20160318</startdate><enddate>20160318</enddate><creator>Nakaoka, Shiho</creator><creator>Sasaki, Kazuki</creator><creator>Ito, Akihiro</creator><creator>Nakao, Yoichi</creator><creator>Yoshida, Minoru</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></search><sort><creationdate>20160318</creationdate><title>A Genetically Encoded FRET Probe to Detect Intranucleosomal Histone H3K9 or H3K14 Acetylation Using BRD4, a BET Family Member</title><author>Nakaoka, Shiho ; Sasaki, Kazuki ; Ito, Akihiro ; Nakao, Yoichi ; Yoshida, Minoru</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a381t-f6b1415c766896c5826314b70894770fd39b909829bfae858516ba531d4022873</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Acetylation</topic><topic>Animals</topic><topic>Cercopithecus aethiops</topic><topic>COS Cells</topic><topic>Fluorescence Resonance Energy Transfer</topic><topic>Gene Expression Regulation</topic><topic>Histone Deacetylase Inhibitors</topic><topic>Histones - metabolism</topic><topic>Humans</topic><topic>Nuclear Proteins - genetics</topic><topic>Nuclear Proteins - metabolism</topic><topic>Transcription Factors - genetics</topic><topic>Transcription Factors - metabolism</topic><topic>Transgenes</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nakaoka, Shiho</creatorcontrib><creatorcontrib>Sasaki, Kazuki</creatorcontrib><creatorcontrib>Ito, Akihiro</creatorcontrib><creatorcontrib>Nakao, Yoichi</creatorcontrib><creatorcontrib>Yoshida, Minoru</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><jtitle>ACS chemical biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nakaoka, Shiho</au><au>Sasaki, Kazuki</au><au>Ito, Akihiro</au><au>Nakao, Yoichi</au><au>Yoshida, Minoru</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Genetically Encoded FRET Probe to Detect Intranucleosomal Histone H3K9 or H3K14 Acetylation Using BRD4, a BET Family Member</atitle><jtitle>ACS chemical biology</jtitle><addtitle>ACS Chem. Biol</addtitle><date>2016-03-18</date><risdate>2016</risdate><volume>11</volume><issue>3</issue><spage>729</spage><epage>733</epage><pages>729-733</pages><issn>1554-8929</issn><eissn>1554-8937</eissn><abstract>Acetylation is a well-characterized histone modification, which plays important roles in controlling epigenetic gene expression, and its malfunction is tightly associated with cancer. By taking advantage of the specific binding of BRD4 to acetylated lysine residues, we developed a FRET-based probe for visualizing histone H3 acetylation in living cells. BRD4, a protein known to be involved in acute myeloid leukemia and nuclear protein in testis midline carcinoma, recognizes the acetylation of histone H3 via its bromodomains. The probe exhibited a significant change in FRET signaling that was dependent on histone H3 acetylation. Mutagenesis studies revealed that an increase in the emission ratio reflected the acetylation of either K9 or K14 of histone H3 within the probe. 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| ispartof | ACS chemical biology, 2016-03, Vol.11 (3), p.729-733 |
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| source | MEDLINE; American Chemical Society Journals |
| subjects | Acetylation Animals Cercopithecus aethiops COS Cells Fluorescence Resonance Energy Transfer Gene Expression Regulation Histone Deacetylase Inhibitors Histones - metabolism Humans Nuclear Proteins - genetics Nuclear Proteins - metabolism Transcription Factors - genetics Transcription Factors - metabolism Transgenes |
| title | A Genetically Encoded FRET Probe to Detect Intranucleosomal Histone H3K9 or H3K14 Acetylation Using BRD4, a BET Family Member |
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