Discrete steps in sensing of beta-lactam antibiotics by the BlaR1 protein of the methicillin-resistant Staphylococcus aureus bacterium.

ABSTRACT: Chemical sensing by cell-surface receptors to effect signal transduction is a ubiquitous biological event. Despite extensive structural biochemical study, detailed knowledge of how signal transduction occurs is largely lacking. We report herein a kinetic and structural study, obtained by stopped-flow IR spectroscopy, of the activation of the BlaR1 receptor of the Staphylococcus aureus bacterium by beta-lactam antibiotics. The cell-surface BlaR1 receptor alerts the bacterium to the presence of beta-lactam antibiotics, resulting in expression of the gene for a beta-lactamase enzyme. This enzyme hydrolytically destroys the remaining beta-lactam antibiotics. IR spectroscopic interrogation of the beta-lactam-BlaR1 receptor reaction has allowed the simultaneous measurement of the chemical events

SUBMITTER: Thumanu K 

PROVIDER: S-EPMC1502283 | biostudies-literature | 2006 Jul

REPOSITORIES: biostudies-literature