Shasha Shi, Juanyu Lin, Yongfei Cai, Jiao Yu, Haiyan Hong, Kunmei Ji, Jennifer S Downey, Xiaodong Lu, Ruichuan Chen, Jiahuai Han, Aidong Han
{"title":"p300/CBP相关因子的二聚体结构","authors":"Shasha Shi, Juanyu Lin, Yongfei Cai, Jiao Yu, Haiyan Hong, Kunmei Ji, Jennifer S Downey, Xiaodong Lu, Ruichuan Chen, Jiahuai Han, Aidong Han","doi":"10.1186/1472-6807-14-2","DOIUrl":null,"url":null,"abstract":"<p>p300/CBP associating factor (PCAF, also known as KAT2B for lysine acetyltransferase 2B) is a catalytic subunit of megadalton metazoan complex ATAC (Ada-Two-A containing complex) for acetylation of histones. However, relatively little is known about the regulation of the enzymatic activity of PCAF.</p><p>Here we present two dimeric structures of the PCAF acetyltransferase (HAT) domain. These dimerizations are mediated by either four-helical hydrophobic interactions or a ?-sheet extension. Our chemical cross-linking experiments in combined with site-directed mutagenesis demonstrated that the PCAF HAT domain mainly forms a dimer in solution through one of the observed interfaces. The results of maltose binding protein (MBP)-pulldown, co-immunoprecipitation and multiangle static light scattering experiments further indicated that PCAF dimeric state is detectable and may possibly exist in vivo.</p><p>Taken together, our structural and biochemical studies indicate that PCAF appears to be a dimer in its functional ATAC complex.</p>","PeriodicalId":498,"journal":{"name":"BMC Structural Biology","volume":"14 1","pages":""},"PeriodicalIF":2.2220,"publicationDate":"2014-01-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1186/1472-6807-14-2","citationCount":"14","resultStr":"{\"title\":\"Dimeric structure of p300/CBP associated factor\",\"authors\":\"Shasha Shi, Juanyu Lin, Yongfei Cai, Jiao Yu, Haiyan Hong, Kunmei Ji, Jennifer S Downey, Xiaodong Lu, Ruichuan Chen, Jiahuai Han, Aidong Han\",\"doi\":\"10.1186/1472-6807-14-2\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p>p300/CBP associating factor (PCAF, also known as KAT2B for lysine acetyltransferase 2B) is a catalytic subunit of megadalton metazoan complex ATAC (Ada-Two-A containing complex) for acetylation of histones. However, relatively little is known about the regulation of the enzymatic activity of PCAF.</p><p>Here we present two dimeric structures of the PCAF acetyltransferase (HAT) domain. These dimerizations are mediated by either four-helical hydrophobic interactions or a ?-sheet extension. Our chemical cross-linking experiments in combined with site-directed mutagenesis demonstrated that the PCAF HAT domain mainly forms a dimer in solution through one of the observed interfaces. The results of maltose binding protein (MBP)-pulldown, co-immunoprecipitation and multiangle static light scattering experiments further indicated that PCAF dimeric state is detectable and may possibly exist in vivo.</p><p>Taken together, our structural and biochemical studies indicate that PCAF appears to be a dimer in its functional ATAC complex.</p>\",\"PeriodicalId\":498,\"journal\":{\"name\":\"BMC Structural Biology\",\"volume\":\"14 1\",\"pages\":\"\"},\"PeriodicalIF\":2.2220,\"publicationDate\":\"2014-01-14\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1186/1472-6807-14-2\",\"citationCount\":\"14\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"BMC Structural Biology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://link.springer.com/article/10.1186/1472-6807-14-2\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"Biochemistry, Genetics and Molecular Biology\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"BMC Structural Biology","FirstCategoryId":"1085","ListUrlMain":"https://link.springer.com/article/10.1186/1472-6807-14-2","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"Biochemistry, Genetics and Molecular Biology","Score":null,"Total":0}
p300/CBP associating factor (PCAF, also known as KAT2B for lysine acetyltransferase 2B) is a catalytic subunit of megadalton metazoan complex ATAC (Ada-Two-A containing complex) for acetylation of histones. However, relatively little is known about the regulation of the enzymatic activity of PCAF.
Here we present two dimeric structures of the PCAF acetyltransferase (HAT) domain. These dimerizations are mediated by either four-helical hydrophobic interactions or a ?-sheet extension. Our chemical cross-linking experiments in combined with site-directed mutagenesis demonstrated that the PCAF HAT domain mainly forms a dimer in solution through one of the observed interfaces. The results of maltose binding protein (MBP)-pulldown, co-immunoprecipitation and multiangle static light scattering experiments further indicated that PCAF dimeric state is detectable and may possibly exist in vivo.
Taken together, our structural and biochemical studies indicate that PCAF appears to be a dimer in its functional ATAC complex.
期刊介绍：
BMC Structural Biology is an open access, peer-reviewed journal that considers articles on investigations into the structure of biological macromolecules, including solving structures, structural and functional analyses, and computational modeling.
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