A multi-layered protein network stabilizes the Escherichia coli FtsZ-ring and modulates constriction dynamics.
A multi-layered protein network stabilizes the Escherichia coli FtsZ-ring and modulates constriction dynamics.
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DOI：
10.1371/journal.pgen.1005128
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发表时间：
2015-04
期刊：
影响因子：
4.5
通讯作者：
Xiao J
中科院分区：
文献类型：
--
作者：
Buss J;Coltharp C;Shtengel G;Yang X;Hess H;Xiao J
原核微管蛋白同源物FtsZ在中细胞处形成环状结构(FtsZ环)。FtsZ环建立了分割面，并使大分子分割机(分割体)的组装成为可能。虽然已经鉴定了该分裂体中的许多分子成分，并对它们的相互作用进行了广泛的描述，但这些蛋白质在该分裂体内的空间组织尚不清楚。因此，驱动分裂体组装、维护和收缩的物理机制仍然难以捉摸。在这里，我们应用基于单分子的超分辨率成像，结合遗传学和生物物理研究，揭示了大肠杆菌中四个重要的分裂体蛋白：FtsZ、ZapA、ZapB和MatP形成的细胞结构的空间组织。我们发现，这些相互作用的蛋白质排列成一个从细胞膜延伸到染色体的多层蛋白质网络，每个网络都具有独特的结构和动态性质。此外，我们发现这个蛋白质网络稳定了FtsZ环，并且出人意料地减缓了细胞的收缩，这表明这个网络在细菌细胞分裂中扮演了一个新的、未被认识到的角色。我们的结果为了解分裂体的结构和功能提供了新的视角，并突出了协调细胞收缩和染色体分离的重要性。细菌细胞分裂是一个高度调控的过程，必须与其他细胞过程(即DNA复制和染色体分离)相协调，以促进忠实的繁殖。在大肠杆菌中，这种调节通常是通过原核细胞微管蛋白同源物FtsZ的聚合来介导的，FtsZ在中间细胞形成环状结构(FtsZ环)。FtsZ环的建立标志着分裂的位置，并使大分子分裂机制(分支体)的组装成为可能。在这里，我们应用基于单分子的超分辨率成像来揭示FtsZ在其调控蛋白：ZapA、ZapB和MatP的背景下的三维结构。我们发现，这四种蛋白质存在于从细胞膜延伸到染色体的多层网络中。这种层次化的组织结构不仅有助于稳定FtsZ环，而且通过影响收缩速率来协调分裂与DNA状态。我们的结果不仅提供了一个关于分裂组的全面的观点，而且还允许获得关于分裂组的结构和功能的新的见解。
The prokaryotic tubulin homolog, FtsZ, forms a ring-like structure (FtsZ-ring) at midcell. The FtsZ-ring establishes the division plane and enables the assembly of the macromolecular division machinery (divisome). Although many molecular components of the divisome have been identified and their interactions extensively characterized, the spatial organization of these proteins within the divisome is unclear. Consequently, the physical mechanisms that drive divisome assembly, maintenance, and constriction remain elusive. Here we applied single-molecule based superresolution imaging, combined with genetic and biophysical investigations, to reveal the spatial organization of cellular structures formed by four important divisome proteins in E. coli: FtsZ, ZapA, ZapB and MatP. We show that these interacting proteins are arranged into a multi-layered protein network extending from the cell membrane to the chromosome, each with unique structural and dynamic properties. Further, we find that this protein network stabilizes the FtsZ-ring, and unexpectedly, slows down cell constriction, suggesting a new, unrecognized role for this network in bacterial cell division. Our results provide new insight into the structure and function of the divisome, and highlight the importance of coordinated cell constriction and chromosome segregation. Bacterial cell division is a highly regulated process that must be coordinated with other cellular processes (i.e. DNA replication and chromosome segregation) to promote faithful reproduction. In Escherichia coli, this regulation is most often mediated through the polymerization of the prokaryotic tubulin homolog, FtsZ, which forms a ring-like structure (FtsZ-ring) at midcell. The establishment of the FtsZ-ring marks the site of division and enables the assembly of the macromolecular division machinery (divisome). Here we applied single-molecule based superresolution imaging to reveal the three-dimensional structure of FtsZ in the context of its regulatory proteins: ZapA, ZapB and MatP. We found that these four proteins exist in a multi-layered network that extends from the cell membrane to the chromosome. This layered organization not only helps to stabilize the FtsZ-ring, but also serves to coordinate division with DNA status by influencing constriction rate. Our results not only provide a comprehensive view of the divisome, but also allow new insight to be garnered regarding the structure and function of the divisome.
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影响因子：
3.6
作者：
Buss J;Coltharp C;Huang T;Pohlmeyer C;Wang SC;Hatem C;Xiao J
通讯作者：
Xiao J
影响因子：
--
作者：
Churchman, L Stirling;Spudich, James A
通讯作者：
Spudich, James A
影响因子：
3.6
作者：
Dajkovic, Alex;Pichoff, Sebastien;Wirtz, Denis
通讯作者：
Wirtz, Denis
影响因子：
3.2
作者：
Galli, Elisa;Gerdes, Kenn
通讯作者：
Gerdes, Kenn
DOI：
10.1002/cphc.201100686
发表时间：
2012-03
期刊：
Chemphyschem : a European journal of chemical physics and physical chemistry
影响因子：
--
作者：
Biteen JS;Goley ED;Shapiro L;Moerner WE
通讯作者：
Moerner WE