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首页> 外文期刊>Biochemistry >Characterization of the beta-Lactam Antibiotic Sensor Domain of the MecR1 Signal Sensor/Transducer Protein from Methicillin-Resistant Staphylococcus aureus
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Characterization of the beta-Lactam Antibiotic Sensor Domain of the MecR1 Signal Sensor/Transducer Protein from Methicillin-Resistant Staphylococcus aureus

机译：耐甲氧西林金黄色葡萄球菌MecR1信号传感器/转导蛋白的β-内酰胺抗生素传感器结构域的表征

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摘要

Methicillin-resistant Staphylococcus aureus (MRSA) has evolved two mechanisms for resistance to beta-lactam antibiotics. One is production of a beta-lactamase, and the other is that of penicillin-binding protein 2a (PBP 2a). The expression of these two proteins is regulated by the bla and mec operons, respectively. BlaR1 and MecR1 are beta-lactam sensor/signal transducer proteins, which experience acylation by beta-lactam antibiotics on the cell surface and transduce the signal into the cytoplasm. The C-terminal surface domain of MecR1 (MecR~s) has been cloned, expressed, and purified to homogeneity. This protein has been characterized by documenting that it has a critical and unusual N~(zeta)-carboxylated lysine at position 394. Furthermore, the kinetics of interactions with beta-lactam antibiotics were evaluated, a process that entails conformational changes for the protein that might be critical for the signal transduction event. Kinetics of acylation of MecR~s are suggestive that signal sensing may be the step where the two systems are substantially different from one another.
机译：耐甲氧西林金黄色葡萄球菌（MRSA）已发展出两种对β-内酰胺类抗生素产生抗药性的机制。一种是产生β-内酰胺酶，另一种是产生青霉素结合蛋白2a（PBP 2a）。这两种蛋白的表达分别受bla和mec操纵子调控。 BlaR1和MecR1是β-内酰胺传感器/信号转导蛋白，它们在细胞表面受到β-内酰胺抗生素的酰化作用，并将信号转导到细胞质中。 MecR1的C末端表面结构域（MecR〜s）已被克隆，表达和纯化至同质。该蛋白质的特征在于，它在394位具有关键和异常的N-（ζ）-羧化赖氨酸。此外，还评估了与β-内酰胺类抗生素相互作用的动力学，该过程需要改变蛋白质的构象，对于信号转导事件可能至关重要。 MecR_s的酰化动力学表明，信号传感可能是两个系统彼此实质不同的步骤。

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