TcaR-ssDNA complex crystal structure reveals new DNA binding mechanism of the MarR family proteins

Yu Ming Chang, Chun Han Ho, Cammy K.M. Chen, Manuel Maestre-Reyna, Masatoshi Weiting Chang-Chien, Andrew H.J. Wang

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)5314-5321
Number of pages8
JournalNucleic Acids Research
Issue number8
Publication statusPublished - Apr 2014

ASJC Scopus subject areas

  • Genetics


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