Signal peptides direct surface proteins to two distinct envelope locations of Staphylococcus aureus
Signal peptides direct surface proteins to two distinct envelope locations of Staphylococcus aureus
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DOI：
10.1038/emboj.2008.185
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发表时间：
2008-10-22
期刊：
影响因子：
11.4
通讯作者：
Schneewind, Olaf
中科院分区：
文献类型：
--
作者：
DeDent, Andrea;Bae, Taeok;Schneewind, Olaf
革兰氏阳性细菌的表面蛋白通过一种需要N端信号肽和C端LPXTG基序分选信号的机制共价连接到细胞壁被膜上。我们在这里表明，金黄色葡萄球菌的表面蛋白到达细菌包膜中的两个不同的目的地，要么以环状分布在每个细胞周围，要么以离散的组装位置分布。环状分布的蛋白质(成团因子A(ClfA)、SpA、纤维连接蛋白结合蛋白B(FnbpB)、丝氨酸-天冬氨酸重复蛋白C(SDRC)和SdrD)含有带有YSIRK/GS基序的信号肽，而指向离散组装位点的蛋白质(金黄色葡萄球菌表面蛋白A(SAA)、SasD、SASF和SASK)则不含有信号肽。带有或不带有YSIRK/GS基序(SASF)的表面蛋白之间的信号肽的相互交换将重组产物定向到替代目的地，而仅改变YSIRK序列的突变不起作用。我们的观察表明，金黄色葡萄球菌将信号肽区分为将蛋白质定位到细胞极点(不含YSIRK/GS的信号肽)或交叉壁(在细胞分裂过程中形成的用于分离新的子细胞的多肽聚糖层)(具有YISRK/GS基序的信号肽)。
Surface proteins of Gram-positive bacteria are covalently linked to the cell wall envelope by a mechanism requiring an N-terminal signal peptide and a C-terminal LPXTG motif sorting signal. We show here that surface proteins of Staphylococcus aureus arrive at two distinct destinations in the bacterial envelope, either distributed as a ring surrounding each cell or as discrete assembly sites. Proteins with ring-like distribution (clumping factor A (ClfA), Spa, fibronectin-binding protein B (FnbpB), serine-aspartate repeat protein C (SdrC) and SdrD) harbour signal peptides with a YSIRK/GS motif, whereas proteins directed to discrete assembly sites (S. aureus surface protein A (SasA), SasD, SasF and SasK) do not. Reciprocal exchange of signal peptides between surface proteins with (ClfA) or without the YSIRK/GS motif (SasF) directed recombinant products to the alternate destination, whereas mutations that altered only the YSIRK sequence had no effect. Our observations suggest that S. aureus distinguishes between signal peptides to address proteins to either the cell pole (signal peptides without YSIRK/GS) or the cross wall, the peptidoglycan layer that forms during cell division to separate new daughter cells (signal peptides with YISRK/GS motif).