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Mechanism of the septal membrane localization of bacterial lipid synthases

细菌脂质合成酶的隔膜膜定位机制

基本信息

批准号：
17570002
负责人：
MATSUMOTO Kouji
金额：
$ 2.3万
依托单位：
SAITAMA UNIVERSITY
依托单位国家：
日本
项目类别：
Grant-in-Aid for Scientific Research (C)
财政年份：
2005
资助国家：
日本
起止时间：
2005 至 2006
项目状态：
已结题

项目摘要

We have found that cardiolipin-rich domains are localized in the septal region and at the poles of Bacillus subtilis membranes and further that phosphatidylethanolamine-rich domains and many lipid synthases are localized on septal region of the membranes. To understand the possible mechanism how the specific phospholipid-rich domains are generated and maintained and what their function may be, we started to examine the mechanism(s) how the lipid synthases are localized to the septal membranes. One approach is to clarify the interactions of the lipid synthases with the proteins and enzymes involved in cell division and also the interactions between the lipid synthases which are expected to form a large complex of the enzymes. Meanwhile we found the enzyme YneS that catalyzes the initial step of glycerophospholipid synthesis, which uses acylphosphate, a new acyl donor produced by PlsX. Hence, we focused on the new enzymes to found an interaction between the two. PlsX interacts with itself. No interaction was found with acyl carrier protein. The other approach is to reveal the region responsible for the septal localization within the enzymes. GFP-fused cardiolipin synthase and phosphatidylglycerophosphate synthase were used as representatives and a series of deletion derivatives were constructed to see the septal localization. Both representatives were found to have amphiphilic α helices at COOH-terminal, probably responsible for the septal localization. Transmembrane helices in phosphatidylglycerophosphate synthase were suggested to be responsible for the septal localization.

我们已经发现，心磷脂丰富的结构域是本地化的隔膜区域和在两极的枯草芽孢杆菌膜，并进一步的磷脂酰乙醇胺丰富的结构域和许多脂质过氧化物酶是本地化的隔膜区域的膜。为了理解特定的富含磷脂的结构域如何产生和维持的可能机制以及它们的功能可能是什么，我们开始研究脂质过氧化物酶如何定位于隔膜的机制。一种方法是阐明脂质过氧化物酶与参与细胞分裂的蛋白质和酶之间的相互作用，以及脂质过氧化物酶之间的相互作用，这些脂质过氧化物酶预期形成酶的大复合物。同时，我们发现了催化甘油磷脂合成的初始步骤的酶YneS，其使用由PlsX产生的新酰基供体酰基磷酸。因此，我们专注于新的酶，以发现两者之间的相互作用。PlsX与自身交互。未发现与酰基载体蛋白的相互作用。另一种方法是揭示酶中负责隔定位的区域。以GFP融合的心磷脂合酶和磷脂酰甘油磷酸合酶为代表，构建了一系列缺失衍生物，观察隔区定位。发现这两个代表在COOH-末端具有两亲性α螺旋，可能负责隔定位。磷脂酰甘油磷酸合酶的跨膜螺旋被认为是负责隔定位。