{"title":"金黄色葡萄球菌SarA单体与DNA复合物的1H、13C和15N共振归属","authors":"Dihong Fu, Bo Duan, Xianzhi Dong, Bin Xia","doi":"10.1007/s12104-023-10140-8","DOIUrl":null,"url":null,"abstract":"<div><p>SarA is a global transcription regulator in <i>S. aureus</i> which regulates the expression of over 120 genes related to quorum sensing, biofilm synthesis, drug resistance and many other important physiological processes during host infection. SarA can bind to the promoter region of <i>agr</i> and other target genes to activate or repress the transcription. The crystal structure of SarA uncovered a MarR protein-like conformation with two symmetrical winged helix domains, while its DNA binding mechanism is still unknown. We have constructed a monomeric DNA binding domain of SarA (SarA<sup>ΔN19</sup>) for the study of the interaction between SarA and DNA with NMR spectroscopy. Here, we report the <sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N NMR assignment of SarA<sup>ΔN19</sup>/DNA complex which is the first step towards further structure and function analysis.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"17 2","pages":"193 - 197"},"PeriodicalIF":0.8000,"publicationDate":"2023-07-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"1H, 13C, and 15N resonance assignments of SarA monomer from Staphylococcus aureus in complex with DNA\",\"authors\":\"Dihong Fu, Bo Duan, Xianzhi Dong, Bin Xia\",\"doi\":\"10.1007/s12104-023-10140-8\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>SarA is a global transcription regulator in <i>S. aureus</i> which regulates the expression of over 120 genes related to quorum sensing, biofilm synthesis, drug resistance and many other important physiological processes during host infection. SarA can bind to the promoter region of <i>agr</i> and other target genes to activate or repress the transcription. The crystal structure of SarA uncovered a MarR protein-like conformation with two symmetrical winged helix domains, while its DNA binding mechanism is still unknown. We have constructed a monomeric DNA binding domain of SarA (SarA<sup>ΔN19</sup>) for the study of the interaction between SarA and DNA with NMR spectroscopy. Here, we report the <sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N NMR assignment of SarA<sup>ΔN19</sup>/DNA complex which is the first step towards further structure and function analysis.</p></div>\",\"PeriodicalId\":492,\"journal\":{\"name\":\"Biomolecular NMR Assignments\",\"volume\":\"17 2\",\"pages\":\"193 - 197\"},\"PeriodicalIF\":0.8000,\"publicationDate\":\"2023-07-05\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biomolecular NMR Assignments\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://link.springer.com/article/10.1007/s12104-023-10140-8\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"BIOPHYSICS\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biomolecular NMR Assignments","FirstCategoryId":"99","ListUrlMain":"https://link.springer.com/article/10.1007/s12104-023-10140-8","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOPHYSICS","Score":null,"Total":0}
1H, 13C, and 15N resonance assignments of SarA monomer from Staphylococcus aureus in complex with DNA
SarA is a global transcription regulator in S. aureus which regulates the expression of over 120 genes related to quorum sensing, biofilm synthesis, drug resistance and many other important physiological processes during host infection. SarA can bind to the promoter region of agr and other target genes to activate or repress the transcription. The crystal structure of SarA uncovered a MarR protein-like conformation with two symmetrical winged helix domains, while its DNA binding mechanism is still unknown. We have constructed a monomeric DNA binding domain of SarA (SarAΔN19) for the study of the interaction between SarA and DNA with NMR spectroscopy. Here, we report the 1H, 13C and 15N NMR assignment of SarAΔN19/DNA complex which is the first step towards further structure and function analysis.
期刊介绍：
Biomolecular NMR Assignments provides a forum for publishing sequence-specific resonance assignments for proteins and nucleic acids as Assignment Notes. Chemical shifts for NMR-active nuclei in macromolecules contain detailed information on molecular conformation and properties.
Publication of resonance assignments in Biomolecular NMR Assignments ensures that these data are deposited into a public database at BioMagResBank (BMRB; http://www.bmrb.wisc.edu/), where they are available to other researchers. Coverage includes proteins and nucleic acids; Assignment Notes are processed for rapid online publication and are published in biannual online editions in June and December.
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