RT Journal Article
SR Electronic
T1 Refutation: <em>Structure and mechanism of the essential two-component signal-transduction system WalKR in Staphylococcus aureus</em>
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 058842
DO 10.1101/058842
A1 Ian R. Monk
A1 Torsten Seemann
A1 Benjamin P. Howden
A1 Timothy P. Stinear
YR 2016
UL http://biorxiv.org/content/early/2016/06/14/058842.abstract
AB In a recent report in Nature Communications, Ji et al., (2016)1 describe the structure of the extracytoplasmic Per-Arnt-Sim (PAS) domain of WalK (WalKEC-PAS), the sensor kinase of the essential two-component regulator WalKR in Staphylococcus aureus1. The authors make two independent walK S. aureus mutants by changing two amino acid residues they postulate from structural analysis and comparisons might be important for signal transduction. We have also been exploring the function of WalKR and were surprised by the striking phenotypic impact of these single amino acid substitutions in the WalK sensor, which are contrary to our own (unpublished) observations.