TY - JOUR
T1 - TcaR-ssDNA complex crystal structure reveals new DNA binding mechanism of the MarR family proteins
AU - Chang, Yu Ming
AU - Ho, Chun Han
AU - Chen, Cammy K.M.
AU - Maestre-Reyna, Manuel
AU - Chang-Chien, Masatoshi Weiting
AU - Wang, Andrew H.J.
N1 - Funding Information:
The authors acknowledge the support of grants from the Institute of Biological Chemistry at Academia Sinica and the National Research Program for Biopharmaceuticals. They thank the National Synchrotron Radiation Research Center of Taiwan and SPring-8 of Japan for beam time allocation. They are also grateful to Hui-Ling Shr and Z. Cheng Don at the Core Facility of X-ray crystallography.
Funding Information:
The Academia Sinica and the National Science Council (Taiwan) [NSC96-3114-P-001-004, NSC97-3114-P-001-001 and NSC99-3113-B-001-001 to A.H.-J.W]. Funding for open access charge: Academia Sinica and National Science Council [NSC99-3113-B-001-001].
PY - 2014/4
Y1 - 2014/4
N2 - 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.
AB - 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.
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U2 - 10.1093/nar/gku128
DO - 10.1093/nar/gku128
M3 - Article
C2 - 24531929
AN - SCOPUS:84899823502
SN - 0305-1048
VL - 42
SP - 5314
EP - 5321
JO - Nucleic Acids Research
JF - Nucleic Acids Research
IS - 8
ER -