FtsZ in Bacterial Cytokinesis: Cytoskeleton and Force Generator All in One

Department of Cell Biology, Box 3709, Duke University Medical Center, Durham, NC 27710, USA.
Microbiology and molecular biology reviews: MMBR (Impact Factor: 14.61). 12/2010; 74(4):504-28. DOI: 10.1128/MMBR.00021-10
Source: PubMed


FtsZ, a bacterial homolog of tubulin, is well established as forming the cytoskeletal framework for the cytokinetic ring. Recent work has shown that purified FtsZ, in the absence of any other division proteins, can assemble Z rings when incorporated inside tubular liposomes. Moreover, these artificial Z rings can generate a constriction force, demonstrating that FtsZ is its own force generator. Here we review light microscope observations of how Z rings assemble in bacteria. Assembly begins with long-pitch helices that condense into the Z ring. Once formed, the Z ring can transition to short-pitch helices that are suggestive of its structure. FtsZ assembles in vitro into short protofilaments that are ∼30 subunits long. We present models for how these protofilaments might be further assembled into the Z ring. We discuss recent experiments on assembly dynamics of FtsZ in vitro, with particular attention to how two regulatory proteins, SulA and MinC, inhibit assembly. Recent efforts to develop antibacterial drugs that target FtsZ are reviewed. Finally, we discuss evidence of how FtsZ generates a constriction force: by protofilament bending into a curved conformation.

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    • "The Z-ring is organized by linear FtsZ-(proto)filaments that in Escherichia coli are anchored to the cell plasma membrane by FtsA and ZipA linker proteins. The assembly and disassembly of protofilaments can happen rapidly on the time-scale of seconds (Erickson et al., 2010). This dynamic nature of the Zring makes it susceptible to regulation by numerous protein factors that can tip the balance between the assembly and disassembly of filaments. "
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    ABSTRACT: To successfully propagate, cells need to coordinate chromosomal replication and segregation with cell division to prevent formation of DNA-less cells and cells with damaged DNA. Here, we review molecular systems in Escherichia coli that are known to be involved in positioning the divisome and chromosome relative to each other. Interestingly, this well-studied micro-organism has several partially redundant mechanisms to achieve this task; none of which are essential. Some of these systems determine the localization of the divisome relative to chromosomes such as SlmA-dependent nucleoid occlusion, some localize the chromosome relative to the divisome such as DNA translocation by FtsK, and some are likely to act on both systems such as the Min system and newly described Ter linkage. Moreover, there is evidence that E. coli harbors other divisome-chromosome coordination systems in addition to those known. The review also discusses the minimal requirements of coordination between chromosomes and cell division proteins needed for cell viability. Arguments are presented that cells can propagate without any dedicated coordination between their chromosomes and cell division machinery at the expense of lowered fitness.
    Frontiers in Microbiology 03/2015; 6. DOI:10.3389/fmicb.2015.00306 · 3.99 Impact Factor
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    • "In effect, the linker pulls the membrane inward as the filament continues to bend and the linker approaches its contour length. Filament ends have been estimated to be approximately 20 nm from the membrane when bent in an intermediate conformation and their center anchored at the membrane [16]. With a contour length of ∼17 nm, the FtsZ linker should be almost fully extended "
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    ABSTRACT: In bacteria, animals, fungi, and many single celled eukaryotes, division is initiated by the formation of a ring of cytoskeletal protein at the nascent division site. In bacteria, the tubulin-like GTPase FtsZ serves as the foundation for the cytokinetic ring. A conserved feature of FtsZ is an intrinsically disordered peptide known as the C-terminal linker. Chimeric experiments suggest the linker acts as a flexible boom allowing FtsZ to associate with the membrane through a conserved C-terminal domain and also modulates interactions both between FtsZ subunits and between FtsZ and modulatory proteins in the cytoplasm.
    Seminars in Cell and Developmental Biology 10/2014; 37. DOI:10.1016/j.semcdb.2014.09.017 · 6.27 Impact Factor
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    • "MreB, the homolog of the eukaryotic actin, has been proposed as the cytoskeletal part of the gliding machinery (Kearns 2007; Mauriello et al. 2010). Also, there may be an association with FtsZ, a protein that is part of the bacterium cytoskeleton and can produce force by itself (Erickson et al. 2010). Linkage between the cytoskeleton and gliding is supported by experimental data with the use of compound A22, which is able to affect the MreB structure and inhibits the gliding motility in Myxobacteria (Nan et al. 2011). "
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    Genome Biology and Evolution 04/2014; 6(4):1013-1030. DOI:10.1093/gbe/evu077 · 4.23 Impact Factor
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Harold Erickson