FisB relies on homo-oligomerization and lipid binding to catalyze membrane fission in bacteria.
FisB relies on homo-oligomerization and lipid binding to catalyze membrane fission in bacteria.
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fish b依靠同质寡聚和脂质结合来催化细菌的膜裂变。
DOI：
10.1371/journal.pbio.3001314
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发表时间：
2021-06
期刊：
影响因子：
9.8
通讯作者：
Karatekin E
中科院分区：
文献类型：
--
作者：
Landajuela A;Braun M;Rodrigues CDA;Martínez-Calvo A;Doan T;Horenkamp F;Andronicos A;Shteyn V;Williams ND;Lin C;Wingreen NS;Rudner DZ;Karatekin E
尽管细菌需要胞质分裂，但对它们的膜分裂机制知之甚少。已知的细菌中唯一的专用膜分裂机制是裂变蛋白B(FisB)，它在枯草杆菌的孢子形成过程中表达，并需要将发育中的孢子释放到母细胞细胞质中。在这里，我们描述了FisB介导的膜分裂的要求。FisB形成由大约12个分子组成的移动簇，在膜分裂时，在吞噬极上让位于一个固定的簇，其中包含大约40个蛋白质。对FisB突变体的分析表明，与酸性脂类结合和同源齐聚都是将FisB靶向吞噬极和膜分裂的关键。使用人造膜和丝状细胞的实验表明，FisB没有固有的感知或诱导膜弯曲的能力，但可以桥接膜。最后，模拟表明，同源寡聚和与膜的反式相互作用足以解释FisB在吞噬后期连接吞噬膜和母细胞膜其余部分的膜颈部积累。总之，我们的结果表明，FisB是一种强大而不寻常的膜分裂蛋白，它依赖于同源齐聚、脂质结合以及吞噬过程中产生的独特的膜拓扑结构来定位和膜断裂，但令人惊讶的是，它不依赖于脂质微域、负曲率脂质或曲率感知。目前对细菌中如何发生膜分裂知之甚少；本研究表明，膜裂变蛋白FisB利用在孢子形成过程中遇到的独特细胞几何形状，通过一种新的机制将其定位到分裂部位，在那里它催化膜断裂。
Little is known about mechanisms of membrane fission in bacteria despite their requirement for cytokinesis. The only known dedicated membrane fission machinery in bacteria, fission protein B (FisB), is expressed during sporulation in Bacillus subtilis and is required to release the developing spore into the mother cell cytoplasm. Here, we characterized the requirements for FisB-mediated membrane fission. FisB forms mobile clusters of approximately 12 molecules that give way to an immobile cluster at the engulfment pole containing approximately 40 proteins at the time of membrane fission. Analysis of FisB mutants revealed that binding to acidic lipids and homo-oligomerization are both critical for targeting FisB to the engulfment pole and membrane fission. Experiments using artificial membranes and filamentous cells suggest that FisB does not have an intrinsic ability to sense or induce membrane curvature but can bridge membranes. Finally, modeling suggests that homo-oligomerization and trans-interactions with membranes are sufficient to explain FisB accumulation at the membrane neck that connects the engulfment membrane to the rest of the mother cell membrane during late stages of engulfment. Together, our results show that FisB is a robust and unusual membrane fission protein that relies on homo-oligomerization, lipid binding, and the unique membrane topology generated during engulfment for localization and membrane scission, but surprisingly, not on lipid microdomains, negative-curvature lipids, or curvature sensing. Little is known about how membrane fission occurs in bacteria; this study suggests that the membrane fission protein FisB exploits the unique cellular geometry encountered during sporulation to enable its localization to the fission site through a novel mechanism, where it catalyzes membrane scission.
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影响因子：
14.9
作者：
Guiziou S;Sauveplane V;Chang HJ;Clerté C;Declerck N;Jules M;Bonnet J
通讯作者：
Bonnet J
影响因子：
64.8
作者：
Douglas, Shawn M.;Dietz, Hendrik;Liedl, Tim;Hoegberg, Bjoern;Graf, Franziska;Shih, William M.
通讯作者：
Shih, William M.
DOI：
10.1126/science.1198701
发表时间：
2011-05-06
期刊：
Science (New York, N.Y.)
影响因子：
--
作者：
Good MC;Zalatan JG;Lim WA
通讯作者：
Lim WA
影响因子：
3.4
作者：
Chen, Zhiming;Atefi, Ehsan;Baumgart, Tobias
通讯作者：
Baumgart, Tobias
影响因子：
28.3
作者：
Ducret, Adrien;Quardokus, Ellen M.;Brun, Yves V.
通讯作者：
Brun, Yves V.