Multiple Interaction Domains in FtsL, a Protein Component of the Widely Conserved Bacterial FtsLBQ Cell Division Complex
Multiple Interaction Domains in FtsL, a Protein Component of the Widely Conserved Bacterial FtsLBQ Cell Division Complex
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DOI：
10.1128/jb.01609-09
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发表时间：
2010-06-01
影响因子：
3.2
通讯作者：
Beckwith, Jon
中科院分区：
文献类型：
--
作者：
Gonzalez, Mark D.;Akbay, Esra A.;Beckwith, Jon
对近400个基因组的生物信息学分析表明，绝大多数细菌具有大肠杆菌蛋白FtsL、FTSB和FtsQ的同源物，这三种蛋白质对细菌的细胞分裂是必不可少的。这三种双结合膜蛋白在体内形成一个亚复合体，独立于其他细胞分裂蛋白。在这里，我们分析了大肠杆菌FtsL的结构域，这些结构域参与了与其他细胞分裂蛋白的相互作用，并对分裂体的组装至关重要。我们发现，正如我们之前用FTSB发现的那样，FtsL在其序列中包装了大量信息，用于与组装途径上下游的蛋白质相互作用。考虑到它们的大小，很可能这两种蛋白质的复合体的唯一功能是充当分裂组组装的支架。
A bioinformatic analysis of nearly 400 genomes indicates that the overwhelming majority of bacteria possess homologs of the Escherichia coli proteins FtsL, FtsB, and FtsQ, three proteins essential for cell division in that bacterium. These three bitopic membrane proteins form a subcomplex in vivo, independent of the other cell division proteins. Here we analyze the domains of E. coli FtsL that are involved in the interaction with other cell division proteins and important for the assembly of the divisome. We show that FtsL, as we have found previously with FtsB, packs an enormous amount of information in its sequence for interactions with proteins upstream and downstream in the assembly pathway. Given their size, it is likely that the sole function of the complex of these two proteins is to act as a scaffold for divisome assembly.