Osorio Aurora, Camarena Laura, Cevallos Miguel Angel, Poggio Sebastian
Departamento de Biología Molecular y Biotecnología, Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México, Mexico City, Mexico.
Programa de Genómica Evolutiva, Centro de Ciencias Genómicas, Universidad Nacional Autónoma de México, Cuernavaca, Morelos, Mexico.
J Bacteriol. 2017 Mar 28;199(8). doi: 10.1128/JB.00811-16. Print 2017 Apr 15.
Bacterial cell division is a complex process that relies on a multiprotein complex composed of a core of widely conserved and generally essential proteins and on accessory proteins that vary in number and identity in different bacteria. The assembly of this complex and, particularly, the initiation of constriction are regulated processes that have come under intensive study. In this work, we characterize the function of DipI, a protein conserved in and that is essential in Our results show that DipI is a periplasmic protein that is recruited late to the division site and that it is required for the initiation of constriction. The recruitment of the conserved cell division proteins is not affected by the absence of DipI, but localization of DipI to the division site occurs only after a mature divisome has formed. Yeast two-hybrid analysis showed that DipI strongly interacts with the FtsQLB complex, which has been recently implicated in regulating constriction initiation. A possible role of DipI in this process is discussed. Bacterial cell division is a complex process for which most bacterial cells assemble a multiprotein complex that consists of conserved proteins and of accessory proteins that differ among bacterial groups. In this work, we describe a new cell division protein (DipI) present only in a group of bacteria but essential in Cells devoid of DipI cannot constrict. Although a mature divisome is required for DipI recruitment, DipI is not needed for recruiting other division proteins. These results, together with the interaction of DipI with a protein complex that has been suggested to regulate cell wall synthesis during division, suggest that DipI may be part of the regulatory mechanism that controls constriction initiation.
细菌细胞分裂是一个复杂的过程，它依赖于一个多蛋白复合体，该复合体由广泛保守且通常必不可少的核心蛋白以及不同细菌中数量和种类各异的辅助蛋白组成。这个复合体的组装，尤其是缢缩的起始，是受到深入研究的调控过程。在这项研究中，我们对DipI的功能进行了表征，DipI是一种在[具体细菌种类1]和[具体细菌种类2]中保守且在[目标细菌种类]中必不可少的蛋白质。我们的结果表明，DipI是一种周质蛋白，它在细胞分裂后期被招募到分裂位点，并且是缢缩起始所必需的。保守的细胞分裂蛋白的招募不受DipI缺失的影响，但DipI定位到分裂位点仅在成熟的分裂体形成之后才会发生。酵母双杂交分析表明，DipI与FtsQLB复合体强烈相互作用，最近的研究表明该复合体与调控缢缩起始有关。本文还讨论了DipI在这一过程中可能发挥的作用。细菌细胞分裂是一个复杂的过程，大多数细菌细胞会组装一个多蛋白复合体，该复合体由保守蛋白和不同细菌群体中存在差异的辅助蛋白组成。在这项研究中，我们描述了一种仅存在于一组细菌中但在[目标细菌种类]中必不可少的新的细胞分裂蛋白（DipI）。缺乏DipI的细胞无法缢缩。尽管DipI的招募需要成熟的分裂体，但招募其他分裂蛋白并不需要DipI。这些结果，连同DipI与一个在分裂过程中被认为调控细胞壁合成的蛋白复合体之间的相互作用，表明DipI可能是控制缢缩起始的调控机制的一部分。
