Bacillus subtilis SepF Binds to the C-Terminus of FtsZ

Król, Ewelina; Kessel, Sebastiaan P. van; Bezouwen, Laura S. van; Kumar, Neeraj; Boekema, Egbert J.; Scheffers, Dirk‐Jan

doi:10.1371/journal.pone.0043293

Cited by 57 publications

(47 citation statements)

References 34 publications

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“…We further observed that the conserved lysine residue (190K) of SepF MTB and the C terminus of FtsZ are important for the SepF-FtsZ interaction in mycobacteria. SepF also binds to the C terminus of FtsZ in B. subtilis (Kró l et al, 2012). P372 present in the C terminus of B. subtilis FtsZ is required for interaction with SepF.…”

Section: Sepf Interacts With Ftsz and Murg In Mycobacteriamentioning

confidence: 99%

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Essential protein SepF of mycobacteria interacts with FtsZ and MurG to regulate cell growth and division

et al. 2015

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Section: Sepf Interacts With Ftsz and Murg In Mycobacteriamentioning

confidence: 99%

“…In addition to FtsA, the repertoire of B. subtilis FtsZ-interacting proteins includes SepF, ZapA and ZapB. SepF binds to the C terminus of FtsZ and is required for proper septum formation (Gündogdu et al, 2011;Ishikawa et al, 2006;Kró l et al, 2012). It can complement for the lack of FtsA.…”

Section: Introductionmentioning

confidence: 99%

Essential protein SepF of mycobacteria interacts with FtsZ and MurG to regulate cell growth and division

et al. 2015

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“…SepF binds directly to the C-terminal domain of FtsZ (6,16). However, the protein has no apparent homology to proteins of known function and the amino acid sequence does not indicate a clear docking site for FtsZ.…”

Section: Resultsmentioning

confidence: 99%

Structural and genetic analyses reveal the protein SepF as a new membrane anchor for the Z ring

Duman

Ishikawa

Celik

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

122

185

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A key step in bacterial cell division is the polymerization of the tubulin homolog FtsZ at midcell. FtsZ polymers are anchored to the cell membrane by FtsA and are required for the assembly of all other cell division proteins. In Gram-positive and cyanobacteria, FtsZ filaments are aligned by the protein SepF, which in vitro polymerizes into large rings that bundle FtsZ filaments. Here we describe the crystal structure of the only globular domain of SepF, located within the C-terminal region. Two-hybrid data revealed that this domain comprises the FtsZ binding site, and EM analyses showed that it is sufficient for ring formation, which is explained by the filaments in the crystals of SepF. Site-directed mutagenesis, gel filtration, and analytical ultracentrifugation indicated that dimers form the basic units of SepF filaments. High-resolution structured illumination microscopy suggested that SepF is membrane associated, and it turned out that purified SepF not only binds to lipid membranes, but also recruits FtsZ. Further genetic and biochemical analyses showed that an amphipathic helix at the N terminus functions as the membrane-binding domain, making SepF a unique membrane anchor for the FtsZ ring. This clarifies why Bacillus subtilis grows without FtsA or the putative membrane anchor EzrA and why bacteria lacking FtsA contain SepF homologs. Both FtsA and SepF use an amphipathic helix for membrane binding. These helices prefer positively curved membranes due to relaxed lipid density; therefore this type of membrane anchor may assist in keeping the Z ring positioned at the strongly curved leading edge of the developing septum.

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“…In vitro, SepF can bind the CTT of either B. subtilis or E. coli FtsZ, indicating that the SepF-FtsZ interaction is dependent on the secondary and tertiary structure of the FtsZ CTT rather than specific amino acid residues (Fig. 1B) (104). Electron micrographs of purified SepF show large regular ring-like structures (76).…”

Section: Sepfmentioning

confidence: 98%

FtsZ Ring Stability: of Bundles, Tubules, Crosslinks, and Curves

2013

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The first step in bacterial cytokinesis is the assembly of a stable but dynamic cytokinetic ring made up of the essential tubulin homolog FtsZ at the future site of division. Although FtsZ and its role in cytokinesis have been studied extensively, the precise architecture of the in vivo medial FtsZ ring (Z ring) is not well understood. Recent advances in superresolution imaging suggest that the Z ring comprises short, discontinuous, and loosely bundled FtsZ polymers, some of which are tethered to the membrane. A diverse array of regulatory proteins modulate the assembly, stability, and disassembly of the Z ring via direct interactions with FtsZ. Negative regulators of FtsZ play a critical role in ensuring the accurate positioning of FtsZ at the future site of division and in maintaining Z ring dynamics by controlling FtsZ polymer assembly/disassembly processes. Positive regulators of FtsZ are essential for tethering FtsZ polymers to the membrane and promoting the formation of stabilizing lateral interactions, permitting assembly of a mature Z ring. The past decade has seen the identification of several factors that promote FtsZ assembly, presumably through a variety of distinct molecular mechanisms. While a few of these proteins are broadly conserved, many positive regulators of FtsZ assembly are limited to small groups of closely related organisms, suggesting that FtsZ assembly is differentially modulated across bacterial species. In this review, we focus on the roles of positive regulators in Z ring assembly and in maintaining the integrity of the cytokinetic ring during the early stages of division. Bacterial cytokinesis is mediated by a macromolecular protein machine that is accurately positioned in space and time during the cell cycle. The earliest defined event during cytokinesis is the assembly of a polymeric FtsZ structure at the site of future division known as the FtsZ ring, or Z ring (1). The Z ring serves as a scaffold for the recruitment of other division proteins (2-5). FtsZ, a tubulin homolog, forms homopolymeric linear protofilaments upon binding GTP, and these filaments subsequently disassemble upon hydrolysis of the bound nucleotide (6-9). Approximately 30% of cellular FtsZ is present in the ring, and fluorescence recovery after photobleaching (FRAP) studies reveal that there is dynamic exchange between FtsZ molecules in the ring polymers and FtsZ monomers or short oligomers in the cytoplasm (10, 11).In Escherichia coli and Bacillus subtilis, cytokinesis can be separated chronologically into the following three steps: (i) assembly and stabilization of the Z ring at the future division site and, following a lag, (ii) recruitment of downstream division proteins, many of which are essential to form a constriction-competent division complex, and lastly, (iii) constriction of the Z ring coordinated with synthesis and splitting of septal peptidoglycan, leading to invagination of the cell membrane and division into two daughter cells (Fig. 1A) (2, 12, 13). The force required for constriction is likely...

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Bacillus subtilis SepF Binds to the C-Terminus of FtsZ

Cited by 57 publications

References 34 publications

Essential protein SepF of mycobacteria interacts with FtsZ and MurG to regulate cell growth and division

Essential protein SepF of mycobacteria interacts with FtsZ and MurG to regulate cell growth and division

Structural and genetic analyses reveal the protein SepF as a new membrane anchor for the Z ring

FtsZ Ring Stability: of Bundles, Tubules, Crosslinks, and Curves

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