Multiple interactions between the transmembrane division proteins of Bacillus subtilis and the role of FtsL instability in divisome assembly
Multiple interactions between the transmembrane division proteins of Bacillus subtilis and the role of FtsL instability in divisome assembly
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DOI：
10.1128/jb.01031-06
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发表时间：
2006-11-01
影响因子：
3.2
通讯作者：
Errington, Jeff
中科院分区：
文献类型：
--
作者：
Daniel, Richard A.;Noirot-Gros, Marie-Francoise;Errington, Jeff
在细菌中，大约11种必需的蛋白质在细胞表面聚集成一个环状结构，从而导致细胞分裂。其中一些蛋白质的主要结构域位于膜外，形成一个我们称之为外环（OR）的组装体。先前对枯草芽孢杆菌分裂的研究表明，四种OR蛋白ftsl、DivIC、DivIB和PBP 2b在组装时相互依赖。这与大肠杆菌中等效蛋白的主要线性途径形成对比。本研究表明枯草芽孢杆菌通路的相互依赖性质可能是由于对FtsL和DivIC稳定性的影响，而DivIB在调节这种转换中起着重要作用。双杂交方法表明，多种蛋白质-蛋白质相互作用有助于OR的组装。DivIC的不同之处在于它只与FtsL产生强烈的相互作用。我们提出了一个由细胞质内环蛋白引导的膜蛋白相互结合形成OR的模型。
About 11 essential proteins assemble into a ring structure at the surface of the cell to bring about cytokinesis in bacteria. Several of these proteins have their major domains located outside the membrane, forming an assembly that we call the outer ring (OR). Previous work on division in Bacillus subtilis has shown that four of the OR proteins-FtsL, DivIC, DivIB, and PBP 2B-are interdependent for assembly. This contrasts with the mainly linear pathway for the equivalent proteins in Escherichia coli. Here we show that the interdependent nature of the B. subtilis pathway could be due to effects on FtsL and DivIC stability and that DivIB is an important player in regulating this turnover. Two-hybrid approaches suggest that a multiplicity of protein-protein interactions contribute to the assembly of the OR. DivIC is unusual in interacting strongly only with FtsL. We propose a model for the formation of the OR through the mutual association of the membrane proteins directed by the cytosolic inner-ring proteins.