https://scholars.lib.ntu.edu.tw/handle/123456789/624882
標題: | TcaR-ssDNA complex crystal structure reveals new DNA binding mechanism of the MarR family proteins | 作者: | Chang Y.-M Ho C.-H Chen C.K.-M MANUEL MAESTRE-REYNA Chang-Chien M.W Wang A.H.-J. |
公開日期: | 2014 | 卷: | 42 | 期: | 8 | 起(迄)頁: | 5314-5321 | 來源出版物: | Nucleic Acids Research | 摘要: | The teicoplanin-associated locus regulator (TcaR) regulates gene expression of proteins on the intercellular adhesion (ica) locus involved in staphylococci poly-N-acetylglucosamine biosynthesis. The absence of TcaR increases poly-N-acetylglucosamine production and promotes biofilm formation. Until recently, the mechanism of multiple antibiotic resistance regulator family protein members, such as TcaR, was restricted to binding double-stranded DNA. However, we recently found that TcaR strongly interacts with single-stranded DNA, which is a new role for this family of proteins. In this study, we report Staphylococcus epidermidis TcaR-single-stranded DNA complex structures. Our model suggests that TcaR and single-stranded DNA form a 61-symmetry polymer composed of TcaR dimers with single-stranded DNA that wraps outside the polymer and 12 nt per TcaR dimer. Single-stranded DNA binding to TcaR involves a large conformational change at the DNA binding lobe. Several point mutations involving the single-stranded DNA binding surface validate interactions between single-stranded DNA and TcaR. Our results extend the novel role of multiple antibiotic resistance regulator family proteins in staphylococci. © 2014 © The Author(s) 2014. Published by Oxford University Press. |
URI: | https://www.scopus.com/inward/record.uri?eid=2-s2.0-84899823502&doi=10.1093%2fnar%2fgku128&partnerID=40&md5=51f36b37554b6b0dc1dffb65e1939cdd https://scholars.lib.ntu.edu.tw/handle/123456789/624882 |
ISSN: | 03051048 | DOI: | 10.1093/nar/gku128 | SDG/關鍵字: | bacterial protein; multidrug resistance protein; single stranded DNA; teicoplanin associated locus regulator; unclassified drug; article; binding site; conformational transition; controlled study; crystal structure; DNA structure; gene expression; nonhuman; point mutation; priority journal; protein DNA binding; protein DNA interaction; protein expression; protein function; protein structure; regulatory mechanism; Staphylococcus epidermidis; Bacterial Proteins; Crystallography, X-Ray; DNA, Single-Stranded; DNA-Binding Proteins; Models, Molecular; Protein Binding; Staphylococcus epidermidis |
顯示於: | 化學系 |
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