Structure-function studies of the staphylococcal methicillin resistance antirepressor MecR2.

@article{Arde2013StructurefunctionSO,
  title={Structure-function studies of the staphylococcal methicillin resistance antirepressor MecR2.},
  author={Pedro Ar{\^e}de and Tiago Botelho and Tibisay Guevara and Isabel Us{\'o}n and Duarte C. Oliveira and F Xavier Gomis-R{\"u}th},
  journal={The Journal of biological chemistry},
  year={2013},
  volume={288 29},
  pages={21267-78}
}
Methicillin resistance in Staphylococcus aureus is elicited by the MecI-MecR1-MecA axis encoded by the mec locus. Recently, MecR2 was also identified as a regulator of mec through binding of the methicillin repressor, MecI. Here we show that plasmid-encoded full-length MecR2 restores resistance in a sensitive S. aureus mecR2 deletion mutant of the resistant strain N315. The crystal structure of MecR2 reveals an N-terminal DNA-binding domain, an intermediate scaffold domain, and a C-terminal… CONTINUE READING