TcaR-ssDNA complex crystal structure reveals new DNA binding mechanism of the MarR family proteins
| Autor: | Andrew H.-J. Wang, Chun Han Ho, Manuel Maestre-Reyna, Masatoshi Weiting Chang-Chien, Yu-Ming Chang, Cammy K.M. Chen |
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| Rok vydání: | 2014 |
| Předmět: |
Genetics
Models Molecular HMG-box Point mutation DNA Single-Stranded Plasma protein binding Biology Crystallography X-Ray DNA-binding protein Cell biology DNA binding site DNA-Binding Proteins chemistry.chemical_compound chemistry Biosynthesis Bacterial Proteins Structural Biology Gene expression Staphylococcus epidermidis DNA Protein Binding |
| Zdroj: | Nucleic Acids Research |
| ISSN: | 1362-4962 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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