Cadaverine Covalently Linked to the Peptidoglycan Serves as the Correct Constituent for the Anchoring Mechanism between the Outer Membrane and Peptidoglycan in Selenomonas ruminantium
Cadaverine Covalently Linked to the Peptidoglycan Serves as the Correct Constituent for the Anchoring Mechanism between the Outer Membrane and Peptidoglycan in Selenomonas ruminantium
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DOI：
10.1128/jb.00106-11
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发表时间：
2011-05-01
影响因子：
3.2
通讯作者：
Kamio, Yoshiyuki
中科院分区：
文献类型：
--
作者：
Kojima, Seiji;Kaneko, Jun;Kamio, Yoshiyuki
在反刍月形单胞菌，严格厌氧和革兰氏阴性细菌，尸胺共价连接的肽聚糖之间的相互作用所需的肽聚糖和S-层同源（SLH）结构域的主要外膜蛋白Mep 45。这里，使用一系列具有NH（3）（+）（CH（2））（n）NH（3）（+）一般结构的二胺，（n = 3至6），我们发现尸胺（n = 5）在获得细胞对外部损伤剂的高抗性方面特异性地充当肽聚糖的最有效成分，并且是Mep 45的SLH结构域与肽聚糖之间的有效相互作用所需的，有利于外膜正确锚定到肽聚糖上。
In Selenomonas ruminantium, a strictly anaerobic and Gram-negative bacterium, cadaverine covalently linked to the peptidoglycan is required for the interaction between the peptidoglycan and the S-layer homologous (SLH) domain of the major outer membrane protein Mep45. Here, using a series of diamines with a general structure of NH(3)(+) (CH(2))(n)NH(3)(+) (n = 3 to 6), we found that cadaverine (n = 5) specifically serves as the most efficient constituent of the peptidoglycan in acquiring the high resistance of the cell to external damage agents and is required for effective interaction between the SLH domain of Mep45 and the peptidoglycan, facilitating the correct anchoring of the outer membrane to the peptidoglycan.