Strauss A, Thumm G, Götz F
Lehrstuhl für Mikrobielle Genetik, Universität Tübingen, 72076 Tübingen, Germany.
J Bacteriol. 1998 Sep;180(18):4960-2. doi: 10.1128/JB.180.18.4960-4962.1998.
Proteins harboring a C-terminal cell wall sorting signal are covalently linked to pentaglycine acceptors within the staphylococcal peptidoglycan. This pentaglycine was modified when the lysostaphin immunity factor (Lif) of Staphylococcus simulans was expressed in Staphylococcus carnosus, likely by the exchange of two glycine residues for serine residues. A reporter protein was efficiently linked to the modified acceptor, indicating that the sorting reaction is not strictly dependent on the wild-type structures of the acceptors.
带有C末端细胞壁分选信号的蛋白质与葡萄球菌肽聚糖中的五甘氨酸受体共价连接。当模仿葡萄球菌的溶葡萄球菌素免疫因子(Lif)在肉葡萄球菌中表达时,这种五甘氨酸发生了修饰,可能是两个甘氨酸残基被丝氨酸残基取代。一种报告蛋白有效地与修饰后的受体相连,这表明分选反应并不严格依赖于受体的野生型结构。