TcaR–ssDNA complex crystal structure reveals new DNA binding mechanism of the MarR family proteins
نویسندگان
چکیده
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.
منابع مشابه
Functional Studies of ssDNA Binding Ability of MarR Family Protein TcaR from Staphylococcus epidermidis
The negative transcription regulator of the ica locus, TcaR, regulates proteins involved in the biosynthesis of poly-N-acetylglucosamine (PNAG). Absence of TcaR increases PNAG production and promotes biofilm formation in Staphylococci. Previously, the 3D structure of TcaR in its apo form and its complex structure with several antibiotics have been analyzed. However, the detailed mechanism of mu...
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Figure 1. Representative MarR homologs and their mode of gene regulation. (A) Structure of MTH313 (3BPX), a MarR homolog of unknown function from Methanobacterium thermoautotrophicum, in complex with the ligand salicylate (shown in magenta). One monomer is shown in gray, the other is colored from amino to carboxyl terminus (blue to red). Note the asymmetrical ligand binding; only ligand binding...
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عنوان ژورنال:
دوره 42 شماره
صفحات -
تاریخ انتشار 2014