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This work has been supported in part by NSF research grant MCB-1252890. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.įunding: A part of this research was conducted at the Center for Nanophase Materials Sciences, which is sponsored at Oak Ridge National Laboratory by the Scientific User Facilities Division, Office of Basic Energy Sciences, U.S. Received: JanuAccepted: Published: August 7, 2014Ĭopyright: © 2014 Bailey et al. Viollier, University of Geneva Medical School, Switzerland In particular, we identify that the Ter macrodomain acts as a landmark for the Z-ring in the presence of MatP, ZapB and ZapA proteins.Ĭitation: Bailey MW, Bisicchia P, Warren BT, Sherratt DJ, Männik J (2014) Evidence for Divisome Localization Mechanisms Independent of the Min System and SlmA in Escherichia coli. coli can divide without the canonical mechanisms for localizing its cytokinetic ring. Furthermore, we provide evidence that this divisome positioning system involves MatP, ZapB, and ZapA proteins. We find that the terminus region of the chromosome moves first to mid-cell where it functions as a positional landmark for the subsequent localization of the Z-ring. Using quantitative fluorescence imaging, we show that slow growing cells lacking both known positioning systems continue to divide accurately at midcell. Here, we explore whether there are additional divisome localization systems in E.
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Currently, two molecular systems, nucleoid occlusion and the Min system, are known to localize the Z-ring. Remarkably, the Z-ring localizes with very high precision at midcell. In particular, we identify that the Ter macrodomain acts as a landmark for the Z-ring in the presence of MatP, ZapB and ZapA proteins.Ĭell division in Escherichia coli begins with the assembly of FtsZ proteins into a ring-like structure, the Z-ring. Our work demonstrates that additional Z-ring localization systems are present in E. Interestingly, even in the absence of Min, SlmA, and the putative Ter macrodomain – Z-ring link, there remains a weak midcell positioning bias for the Z-ring. Removal of either the MatP, ZapB, or ZapA proteins significantly affects the accuracy and precision of Z-ring positioning relative to the nucleoid center in these cells in accordance with the idea that these proteins link the Ter macrodomain and the Z-ring. We determine that Z-ring formation begins shortly after the arrival of the Ter macrodomain at the nucleoid center. We find that the initial Z-ring assembly occurs over the center of the nucleoid instead of nucleoid-free regions under these conditions. Using quantitative fluorescence imaging we show that slow growing cells lacking functional Min and SlmA nucleoid occlusion systems continue to divide preferentially at midcell. coli divisome with respect to the cell center. Here, we address the question of whether there are additional positioning systems that are capable of localizing the E. coli, nucleoid occlusion is mediated by the SlmA proteins. Positioning of the Z-ring at midcell is thought to be coordinated by two regulatory systems, nucleoid occlusion and the Min system. Cell division in Escherichia coli starts with assembly of FtsZ protofilaments into a ring-like structure, the Z-ring.