scholarly journals ZapG (YhcB/DUF1043), a novel cell division protein in gamma-proteobacteria linking the Z-ring to septal peptidoglycan synthesis

2021 ◽  
pp. 100700
Author(s):  
Jitender Mehla ◽  
George Liechti ◽  
Randy M. Morgenstein ◽  
J. Harry Caufield ◽  
Ali Hosseinnia ◽  
...  
Keyword(s):  
Cell Division ◽  
Peptidoglycan Synthesis ◽  
Gamma Proteobacteria ◽  
Z Ring ◽  
Cell Division Protein

scholarly journals LocZ Is a New Cell Division Protein Involved in Proper Septum Placement in Streptococcus pneumoniae

mBio ◽  
2014 ◽  
Vol 6 (1) ◽  
Author(s):  
Nela Holečková ◽  
Linda Doubravová ◽  
Orietta Massidda ◽  
Virginie Molle ◽  
Karolína Buriánková ◽  
...  
Keyword(s):  
Cell Division ◽  
Streptococcus Pneumoniae ◽  
Protein Kinase ◽  
Bacterial Cell Division ◽  
Content Type ◽  
Daughter Cells ◽  
Division Site ◽  
Z Ring ◽  
Specific Shape ◽  
Cell Division Protein

ABSTRACTHow bacteria control proper septum placement at midcell, to guarantee the generation of identical daughter cells, is still largely unknown. Although different systems involved in the selection of the division site have been described in selected species, these do not appear to be widely conserved. Here, we report that LocZ (Spr0334), a newly identified cell division protein, is involved in proper septum placement inStreptococcus pneumoniae. We show thatlocZis not essential but that its deletion results in cell division defects and shape deformation, causing cells to divide asymmetrically and generate unequally sized, occasionally anucleated, daughter cells. LocZ has a unique localization profile. It arrives early at midcell, before FtsZ and FtsA, and leaves the septum early, apparently moving along with the equatorial rings that mark the future division sites. Consistently, cells lacking LocZ also show misplacement of the Z-ring, suggesting that it could act as a positive regulator to determine septum placement. LocZ was identified as a substrate of the Ser/Thr protein kinase StkP, which regulates cell division in S. pneumoniae. Interestingly, homologues of LocZ are found only in streptococci, lactococci, and enterococci, indicating that this close phylogenetically related group of bacteria evolved a specific solution to spatially regulate cell division.IMPORTANCEBacterial cell division is a highly ordered process regulated in time and space. Recently, we reported that the Ser/Thr protein kinase StkP regulates cell division in Streptococcus pneumoniae, through phosphorylation of several key proteins. Here, we characterized one of the StkP substrates, Spr0334, which we named LocZ. We show that LocZ is a new cell division protein important for proper septum placement and likely functions as a marker of the cell division site. Consistently, LocZ supports proper Z-ring positioning at midcell. LocZ is conserved only among streptococci, lactococci, and enterococci, which lack homologues of the Min and nucleoid occlusion effectors, indicating that these bacteria adapted a unique mechanism to find their middle, reflecting their specific shape and symmetry.

scholarly journals Influence of CrgA on Assembly of the Cell Division Protein FtsZ during Development of Streptomyces coelicolor

2006 ◽  
Vol 188 (4) ◽  
pp. 1540-1550 ◽  
Author(s):  
Ricardo Del Sol ◽  
Jonathan G. L. Mullins ◽  
Nina Grantcharova ◽  
Klas Flärdh ◽  
Paul Dyson
Keyword(s):  
Cell Division ◽  
Streptomyces Coelicolor ◽  
Orthologous Gene ◽  
Integral Membrane Protein ◽  
Origin Of Replication ◽  
Small Proteins ◽  
Aerial Hyphae ◽  
Z Ring ◽  
Cell Division Protein ◽  
Conserved Gene

ABSTRACT The product of the crgA gene of Streptomyces coelicolor represents a novel family of small proteins. A single orthologous gene is located close to the origin of replication of all fully sequenced actinomycete genomes and borders a conserved gene cluster implicated in cell growth and division. In S. coelicolor, CrgA is important for coordinating growth and cell division in sporogenic hyphae. In this study, we demonstrate that CrgA is an integral membrane protein whose peak expression is coordinated with the onset of development of aerial hyphae. The protein localizes to discrete foci away from growing hyphal tips. Upon overexpression, CrgA localizes to apical syncytial cells of aerial hyphae and inhibits the formation of productive cytokinetic rings of the bacterial tubulin homolog FtsZ, leading to proteolytic turnover of this major cell division determinant. In the absence of known prokaryotic cell division inhibitors in actinomycetes, CrgA may have an important conserved function influencing Z-ring formation in these bacteria.

scholarly journals The Stress-Active Cell Division Protein ZapE Alters FtsZ Filament Architecture to Facilitate Division in Escherichia coli

2021 ◽  
Vol 12 ◽  
Author(s):  
Eric C. DiBiasio ◽  
Rebecca A. Dickinson ◽  
Catherine E. Trebino ◽  
Colby N. Ferreira ◽  
Josiah J. Morrison ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
High Temperature ◽  
Environmental Stress ◽  
Atp Hydrolysis ◽  
Major Protein ◽  
Bacterial Cells ◽  
Z Ring ◽  
Cell Division Protein

During pathogenic infections, bacterial cells experience environmental stress conditions, including low oxygen and thermal stress. Bacterial cells proliferate during infection and divide by a mechanism characterized by the assembly of a large cytoskeletal structure at the division site called the Z-ring. The major protein constituting the Z-ring is FtsZ, a tubulin homolog and GTPase that utilizes the nucleotide to assemble into dynamic polymers. In Escherichia coli, many cell division proteins interact with FtsZ and modulate Z-ring assembly, while others direct cell wall insertion and peptidoglycan remodeling. Here, we show that ZapE, an ATPase that accumulates during late constriction, directly interacts with FtsZ and phospholipids in vitro. In the presence of adenosine triphosphate (ATP), ZapE induces bundling of GTP-induced FtsZ polymers; however, ZapE also binds FtsZ in the absence of GTP. The ZapE mutant protein ZapE(K84A), which is defective for ATP hydrolysis, also interacts with FtsZ and induces FtsZ filament bundling. In vivo, cultures of zapE deletion cells contain a low percentage of filamentous cells, suggesting that they have a modest division defect; however, they are able to grow when exposed to stress, such as high temperature and limited oxygen. When combined with the chromosomal deletion of minC, which encodes an FtsZ disassembly factor, ΔzapE ΔminC cells experience growth delays that slow proliferation at high temperature and prevent recovery. This synthetic slow growth phenotype after exposure to stress suggests that ZapE may function to ensure proliferation during and after stress, and this is exacerbated when cells are also deleted for minC. Expression of either ZapE or ZapE(K84A) complements the aberrant growth phenotypes in vivo suggesting that the division-associated role of ZapE does not require ZapE ATP hydrolysis. These results support that ZapE is a stress-regulated cell division protein that interacts directly with FtsZ and phospholipids, promoting growth and division after exposure to environmental stress.

scholarly journals An essential Staphylococcus aureus cell division protein directly regulates FtsZ dynamics

eLife ◽  
2018 ◽  
Vol 7 ◽  
Author(s):  
Prahathees J Eswara ◽  
Robert S Brzozowski ◽  
Marissa G Viola ◽  
Gianni Graham ◽  
Catherine Spanoudis ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Cell Division ◽  
Cell Lysis ◽  
Regulatory Proteins ◽  
Binary Fission ◽  
Gtpase Activity ◽  
Human Pathogen ◽  
The Core ◽  
Z Ring ◽  
Cell Division Protein

Binary fission has been well studied in rod-shaped bacteria, but the mechanisms underlying cell division in spherical bacteria are poorly understood. Rod-shaped bacteria harbor regulatory proteins that place and remodel the division machinery during cytokinesis. In the spherical human pathogen Staphylococcus aureus, we found that the essential protein GpsB localizes to mid-cell during cell division and co-constricts with the division machinery. Depletion of GpsB arrested cell division and led to cell lysis, whereas overproduction of GpsB inhibited cell division and led to the formation of enlarged cells. We report that S. aureus GpsB, unlike other Firmicutes GpsB orthologs, directly interacts with the core divisome component FtsZ. GpsB bundles and organizes FtsZ filaments and also stimulates the GTPase activity of FtsZ. We propose that GpsB orchestrates the initial stabilization of the Z-ring at the onset of cell division and participates in the subsequent remodeling of the divisome during cytokinesis.

scholarly journals The Escherichia coli Cell Division Protein FtsW Is Required To Recruit Its Cognate Transpeptidase, FtsI (PBP3), to the Division Site

2002 ◽  
Vol 184 (4) ◽  
pp. 904-912 ◽  
Author(s):  
Keri L. N. Mercer ◽  
David S. Weiss
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Subcellular Location ◽  
Bacterial Cell Division ◽  
Penicillin Binding Protein ◽  
Peptidoglycan Synthesis ◽  
Division Site ◽  
Cell Division Protein ◽  
Septal Localization ◽  
Almost All

ABSTRACT The bacterial cell division protein FtsW has been suggested to perform two functions: stabilize the FtsZ cytokinetic ring, and facilitate septal peptidoglycan synthesis by the transpeptidase FtsI (penicillin-binding protein 3). We show here that depleting Escherichia coli cells of FtsW had little effect on the abundance of FtsZ rings but abrogated recruitment of FtsI to potential division sites. Analysis of FtsW localization confirmed and extended these results; septal localization of FtsW required FtsZ, FtsA, FtsQ, and FtsL but not FtsI. Thus, FtsW is a late recruit to the division site and is essential for subsequent recruitment of its cognate transpeptidase FtsI but not for stabilization of FtsZ rings. We suggest that a primary function of FtsW homologues—which are found in almost all bacteria and appear to work in conjunction with dedicated transpeptidases involved in division, elongation, or sporulation—is to recruit their cognate transpeptidases to the correct subcellular location.

scholarly journals ZapE Is a Novel Cell Division Protein Interacting with FtsZ and Modulating the Z-Ring Dynamics

mBio ◽  
2014 ◽  
Vol 5 (2) ◽  
Author(s):  
Benoit S. Marteyn ◽  
Gouzel Karimova ◽  
Andrew K. Fenton ◽  
Anastasia D. Gazi ◽  
Nicholas West ◽  
...  
Keyword(s):  
Cell Division ◽  
Bacterial Cell ◽  
Dependent Manner ◽  
Bacterial Cell Division ◽  
Low Oxygen ◽  
Ftsz Ring ◽  
Division Process ◽  
Z Ring ◽  
Cell Division Protein

ABSTRACTBacterial cell division requires the formation of a mature divisome complex positioned at the midcell. The localization of the divisome complex is determined by the correct positioning, assembly, and constriction of the FtsZ ring (Z-ring). Z-ring constriction control remains poorly understood and (to some extent) controversial, probably due to the fact that this phenomenon is transient and controlled by numerous factors. Here, we characterize ZapE, a novel ATPase found in Gram-negative bacteria, which is required for growth under conditions of low oxygen, while loss ofzapEresults in temperature-dependent elongation of cell shape. We found that ZapE is recruited to the Z-ring during late stages of the cell division process and correlates with constriction of the Z-ring. Overexpression or inactivation ofzapEleads to elongation ofEscherichia coliand affects the dynamics of the Z-ring during division.In vitro, ZapE destabilizes FtsZ polymers in an ATP-dependent manner.IMPORTANCEBacterial cell division has mainly been characterizedin vitro. In this report, we could identify ZapE as a novel cell division protein which is not essentialin vitrobut is required during an infectious process. The bacterial cell division process relies on the assembly, positioning, and constriction of FtsZ ring (the so-called Z-ring). Among nonessential cell division proteins recently identified, ZapE is the first in which detection at the Z-ring correlates with its constriction. We demonstrate that ZapE abundance has to be tightly regulated to allow cell division to occur; absence or overexpression of ZapE leads to bacterial filamentation. AszapEis not essential, we speculate that additional Z-ring destabilizing proteins transiently recruited during late cell division process might be identified in the future.

scholarly journals FtsZ assembles the bacterial cell division machinery by a diffusion-and-capture mechanism

2018 ◽  
Author(s):  
Natalia Baranova ◽  
Philipp Radler ◽  
Víctor M. Hernández-Rocamora ◽  
Carlos Alfonso ◽  
Mar López-Pelegrín ◽  
...  
Keyword(s):  
Cell Division ◽  
Bacterial Cell ◽  
Bacterial Cell Division ◽  
Peptidoglycan Synthesis ◽  
Division Site ◽  
Spatiotemporal Information ◽  
Capture Mechanism ◽  
Z Ring ◽  
Membrane Bound ◽  
Transient Interactions

AbstractThe mechanism of bacterial cell division is largely unknown. The protein machinery performing cell division is organized by FtsZ, a tubulin-homolog that forms treadmilling filaments at the cell division site. Treadmilling is thought to actively move proteins around the cell thereby distributing peptidoglycan synthesis to make two new cell poles. To understand this process, we reconstituted part of the bacterial cell division machinery using the purified components FtsZ, FtsA and truncated transmembrane proteins essential for cell division. We found that membrane-bound cytosolic peptides of FtsN and FtsQ co-migrated with treadmilling FtsZ-FtsA filaments. Remarkably, rather than moving in a directed fashion, individual peptides followed FtsZ filaments by a diffusion-and-capture mechanism. Our work provides a mechanism for how the Z-ring dynamically recruits divisome proteins and highlights the importance of transient interactions for the self-organization of complex biological structures. We propose that this mechanism is used more widely to organize and transmit spatiotemporal information in living cells.One Sentence SummaryFtsZ treadmilling assembles bacterial division machinery by diffusion-and-capture mechanism.

scholarly journals A conserved cell division protein directly regulates FtsZ dynamics in filamentous and unicellular actinobacteria

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Félix Ramos-León ◽  
Matthew J Bush ◽  
Joseph W Sallmen ◽  
Govind Chandra ◽  
Jake Richardson ◽  
...  
Keyword(s):  
Cell Division ◽  
Bacterial Cell ◽  
Mycobacterium Smegmatis ◽  
Bacterial Cell Division ◽  
Z Ring ◽  
Cell Division Protein ◽  
Ring Architecture ◽  
Contractile Structure

Bacterial cell division is driven by the polymerization of the GTPase FtsZ into a contractile structure, the so-called Z-ring. This essential process involves proteins that modulate FtsZ dynamics and hence the overall Z-ring architecture. Actinobacteria like Streptomyces and Mycobacterium lack known key FtsZ-regulators. Here we report the identification of SepH, a conserved actinobacterial protein that directly regulates FtsZ dynamics. We show that SepH is crucially involved in cell division in Streptomyces venezuelae and that it binds FtsZ via a conserved helix-turn-helix motif, stimulating the assembly of FtsZ protofilaments. Comparative in vitro studies using the SepH homolog from Mycobacterium smegmatis further reveal that SepH can also bundle FtsZ protofilaments, indicating an additional Z-ring stabilizing function in vivo. We propose that SepH plays a crucial role at the onset of cytokinesis in actinobacteria by promoting the assembly of FtsZ filaments into division-competent Z-rings that can go on to mediate septum synthesis.

scholarly journals Chlamydial MreB Directs Cell Division and Peptidoglycan Synthesis in Escherichia coli in the Absence of FtsZ Activity

mBio ◽  
2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Dev K. Ranjit ◽  
George W. Liechti ◽  
Anthony T. Maurelli
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Morphological Changes ◽  
Content Type ◽  
E Coli ◽  
Obligate Intracellular ◽  
Peptidoglycan Synthesis ◽  
Division Site ◽  
A Cell ◽  
Cell Division Protein

ABSTRACT Cell division is the ultimate process for the propagation of bacteria, and FtsZ is an essential protein used by nearly all bacteria for this function. Chlamydiae belong to a small group of bacteria that lack the universal cell division protein FtsZ but still divide by binary fission. Chlamydial MreB is a member of the shape-determining MreB/Mbl family of proteins responsible for rod shape morphology in Escherichia coli. Chlamydia also encodes a homolog of RodZ, an MreB assembly cytoskeletal protein that links MreB to cell wall synthesis proteins. We hypothesized that MreB directs cell division in Chlamydia and that chlamydial MreB could replace FtsZ function for cell division in E. coli. Overexpression of chlamydial mreB-rodZ in E. coli induced prominent morphological changes with production of large swollen or oval bacteria, eventually resulting in bacterial lysis. Low-level expression of chlamydial mreB-rodZ restored viability of a lethal ΔmreB mutation in E. coli, although the bacteria lost their typical rod shape and grew as rounded cells. When FtsZ activity was inhibited by overexpression of SulA in the ΔmreB mutant of E. coli complemented with chlamydial mreB-rodZ, spherical E. coli grew and divided. Localization studies using a fluorescent fusion chlamydial MreB protein indicated that chlamydial RodZ directs chlamydial MreB to the E. coli division septum. These results demonstrate that chlamydial MreB, in partnership with chlamydial RodZ, acts as a cell division protein. Our findings suggest that an mreB-rodZ-based mechanism allows Chlamydia to divide without the universal division protein FtsZ. IMPORTANCE The study of Chlamydia growth and cell division is complicated by its obligate intracellular nature and biphasic lifestyle. Chlamydia also lacks the universal division protein FtsZ. We employed the cell division system of Escherichia coli as a surrogate to identify chlamydial cell division proteins. We demonstrate that chlamydial MreB, together with chlamydial RodZ, forms a cell division and growth complex that can replace FtsZ activity and support cell division in E. coli. Chlamydial RodZ plays a major role in directing chlamydial MreB localization to the cell division site. It is likely that the evolution of chlamydial MreB and RodZ to form a functional cell division complex allowed Chlamydia to dispense with its FtsZ-based cell division machinery during genome reduction. Thus, MreB-RodZ represents a possible mechanism for cell division in other bacteria lacking FtsZ.

Sign in / Sign up

Export Citation Format

Share Document