Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10748237 | Biochemical and Biophysical Research Communications | 2016 | 20 Pages |
Abstract
Two-component system SaeRS of Staphylococcus regulates virulence factor expression through phosphorylation of the DNA-binding regulator SaeR by the sensor histidine kinase SaeS. Here crystal structures of the DNA-binding domain (DBD) of SaeR from two Staphylococcal species Staphylococcus epidermidis and Staphylococcus aureus were determined and showed similar folds. Analyzing the DNA binding activity of three mutants of SeSaeR, we observed that Thr217 is important in binding to the phosphate group of DNA and Trp219 may interact with the base pairs. Additionally, the tandem arrangement of DBD may represent a possible way for SaeR oligomerization on DNA.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Tzu-Ping Ko, Cheng-Yang Huang, Tung-Ju Hsieh, Sheng-Chia Chen, Yu-Ren Chen, Chia-Shin Yang, Hao-Cheng Kuo, Wen-Lung Wang, Tzu-Hung Hsiao, Ching-Heng Lin, Yeh Chen,