FtsZ

FtsZ is a protein encoded by the ftsZ gene that assembles into a ring
at the future site of bacterial cell division. FtsZ is a prokaryotic
Cell division protein FtsZ
homologue of the eukaryotic protein tubulin. The initials FtsZ mean Identifiers
"Filamenting temperature-sensitive mutant Z." The hypothesis was Symbol FtsZ
that cell division mutants of E. coli would grow as filaments due to
the inability of the daughter cells to separate from one another. FtsZ is InterPro IPR000158 (https://www.e
found in almost all bacteria, many archaea, all chloroplasts and some bi.ac.uk/interpro/entry/IP
mitochondria, where it is essential for cell division. FtsZ assembles the R000158)
cytoskeletal scaffold of the Z ring that, along with additional proteins, CATH 1fsz (http://www.cathdb.in
constricts to divide the cell in two. fo/pdb/1fsz)
SCOPe 1fsz (https://scop.berkele
y.edu/pdb/code=1fsz) /
Contents SUPFAM (http://supfam.o
History rg/SUPERFAMILY/cgi-bin/
search.cgi?search_field=
Function
1fsz)
The contractile ring
Septal localization and intracellular signaling CDD cd02201 (https://www.ncb
i.nlm.nih.gov/Structure/cd
Communicating distress
d/cddsrv.cgi?uid=cd0220
Preventing DNA damage
1)
Clinical significance
See also FtsZ, C-terminal sandwich
References Identifiers
Symbol FtsZ_C
Pfam PF12327 (http://pfam.xfam.
History
org/family?acc=PF12327)

In the 1960s scientists screened for temperature sensitive mutations InterPro IPR024757 (https://www.eb
that blocked cell division at 42° C. The mutant cells divided i.ac.uk/interpro/entry/IPR02
normally at 30°, but failed to divide at 42°. Continued growth 4757)
without division produced long filamentous cells (Filamenting
Available protein structures:
temperature sensitive). Several such mutants were discovered and
mapped to a locus originally named ftsA, which could be one or Pfam structures (http://pfam.xfam.or
g/family/PF12327?tab=pdbBlo
more genes. In 1980 Lutkenhaus and Donachie[1] showed that
ck) / ECOD (http://prodata.swm
several of these mutations mapped to one gene, ftsA, but one well-
ed.edu/ecod/complete/searc
characterized mutant, PAT84, originally discovered by Hirota et
h?kw=PF12327)
al,[2] mapped to a separate, adjacent gene. They named this cell
division gene ftsZ. In 1991 Bi and Lutkenhaus used immunogold PDB RCSB PDB (http://www.rcsb.or
electron microscopy to show that FtsZ localized to the invaginating g/pdb/search/smartSubquery.d
o?smartSearchSubtype=PfamI
septum at midcell.[3] Subsequently, the Losick and Margolin groups
dQuery&pfamID=PF12327);
used immuno-fluorescence microscopy[4] and GFP fusions[5] to
PDBe (https://www.ebi.ac.uk/p
show that FtsZ assembled Z rings early in the cell cycle, well before dbe/entry/search/index?pfam_
accession:PF12327); PDBj (htt
the septum began to constrict. Other division proteins then assemble ps://pdbj.org/searchFor?query
onto the Z ring and constriction occurs in the last part of the cell =PF12327)
cycle. PDBsum structure summary (https://ww
w.ebi.ac.uk/thornton-srv/datab
In 1992-3 three labs independently discovered that FtsZ was related ases/cgi-bin/pdbsum/GetPfam
to eukaryotic tubulin, which is the protein subunit that assembles Str.pl?pfam_id=PF12327)
into microtubules[6][7][8]. This was the first discovery that bacteria
have homologs of eukaryotic cytoskeletal proteins. Later work Cell division protein FtsZ
showed that FtsZ was present in, and essential for, cell division in
almost all bacteria and in many but not all archaea.

Mitochondria and chloroplasts are eukaryotic organelles that

originated as bacterial endosymbionts, so there was much interest in
whether they use FtsZ for division. Chloroplast FtsZ was first
discovered by Osteryoung[9], and it is now known that all
chloroplasts use FtsZ for division. Mitochondrial FtsZ was
discovered by Beech[10] in an alga; FtsZ is used for mitochondrial
division in some eukaryotes, while others have replaced it with a
dynamin-based machinery.

Function Molecular Structure of FtsZ (PDB

1fsz).
During cell division, FtsZ is the first protein to move to the division
site, and is essential for recruiting other proteins that produce a new Identifiers
cell wall (septum) between the dividing cells. FtsZ's role in cell Organism Escherichia coli (https://w
division is analogous to that of tubulin in eukaryotic cell division, ww.ncbi.nlm.nih.gov/Taxo
but, unlike the actin-myosin ring in eukaryotes, FtsZ has no known nomy/Browser/wwwtax.cg
motor protein associated with it. The origin of the cytokinetic force, i?name=%27%27Escheri
thus, remains unclear, but it is believed that the localized synthesis
chia+coli%27%27&rn=1)
of new cell wall produces at least part of this force.[11] In liposomes
Osawa (2009) showed FtsZ is capable of exerting a contractile force Symbol ftsZ
with no other proteins present.[12] UniProt P0A9A6 (https://www.unip
rot.org/uniprot/P0A9A6)
Erickson (2009) proposed how the roles of tubulin-like proteins and
actin-like proteins in cell division became reversed in an Search for

evolutionary mystery.[13] The use of the FtsZ ring in dividing Structures Swiss-model (https://swissm
chloroplasts and some mitochondria further establishes their odel.expasy.org/repository/u
prokaryotic ancestry.[14] L-form bacteria that lack a cell wall do not niprot/P0A9A6)
require FtsZ for division, which implies that bacteria may have Domains InterPro (https://www.ebi.ac.u
retained components of an ancestral mode of cell division.[15] k/interpro/protein/P0A9A6)

Much is known about the dynamic polymerization activities of tubulin and microtubules, but little is known
about these activities in FtsZ. While it is known that single-stranded tubulin protofilaments form into 13
stranded microtubules, the multistranded structure of the FtsZ-containing Z-ring is not known. It is only
speculated that the structure consists of overlapping protofilaments. Nevertheless, recent work with purified
FtsZ on supported lipid bilayers as well as imaging FtsZ in living bacterial cells revealed that FtsZ
protofilaments have polarity and move in one direction by treadmilling [16](see also below).

Recently, proteins similar to tubulin and FtsZ have been discovered in large plasmids found in Bacillus
species. They are believed to function as components of segrosomes, which are multiprotein complexes that
partition chromosomes/plasmids in bacteria. The plasmid homologs of tubulin/FtsZ seem to have conserved
the ability to polymerize into filaments.
The contractile ring

FtsZ has the ability to bind to GTP and also exhibits a GTPase domain that
allows it to hydrolyze GTP to GDP and a phosphate group. In vivo, FtsZ
forms filaments with a repeating arrangement of subunits, all arranged head-
to-tail.[17] These filaments form a ring around the longitudinal midpoint, or
septum, of the cell. This ring is called the Z-ring.
Inhibition of FtsZ disrupts
The GTP hydrolyzing activity of the protein is not essential to the formation septum formation, resulting
of filaments or cell division. Mutants defective in GTPase activity often still in filamentation of bacterial
divide, but sometimes form twisted and disordered septa. It is unclear as to cells (top right of electron
whether FtsZ actually provides the physical force that results in division or micrograph).
serves as a marker for other proteins to execute division.

If FtsZ does provide force that divides the cell, it may do so through
the relative movement of subunits. Computer models and in vivo
measurements suggest that single FtsZ filaments cannot sustain a
length more than 30 subunits long. In this model, FtsZ scission force
comes from the relative lateral movement of subunits.[18] Lines of
FtsZ would line up together parallel and pull on each other creating a
"cord" of many strings that tightens itself.

In other models, FtsZ does not provide the contractile force but
provides the cell a spatial scaffold for other proteins to execute the
division of the cell. This is akin to the creating of a temporary
structure by construction workers to access hard-to-reach places of a
building. The temporary structure allows unfettered access and The Z-ring forms from smaller
ensures that the workers can reach all places. If the temporary subunits of FtsZ filaments. These
structure is not correctly built, the workers will not be able to reach filaments may pull on each other and
certain places, and the building will be deficient. tighten to divide the cell.

The scaffold theory is supported by information that shows that the

formation of the ring and localization to the membrane requires the concerted
action of a number of accessory proteins. ZipA or the actin homologue FtsA
permit initial FtsZ localization to the membrane.[19] Following localization to
the membrane, division proteins of the Fts family are recruited for ring
assembly.[20] Many of these proteins, such as FtsW, FtsK, and FtsQ are
involved in stabilization of the Z ring and may also be active participants in
the scission event. The timing of Z-ring formation suggests the possibility of a
spatial or temporal signal that permits the formation of FtsZ filaments.

Recent super-resolution imaging in several species supports a dynamic

scaffold model, in which small clusters of FtsZ protofilaments or Super-resolution image of Z-
protofilament bundles move unidirectionally around the ring's circumference rings (green) at different
by treadmilling, anchored to the membrane by FtsA and other FtsZ-specific stages of constriction in two
membrane tethers. [21][22] The speed of treadmilling depends on the rate of E. coli cells.
GTP hydrolysis within the FtsZ protofilaments, but in Escherichia coli,
synthesis of the division septum remains the rate limiting step for
cytokinesis.[23] The treadmilling action of FtsZ is required for proper synthesis of the division septum by septal
peptidoglycan synthesis enzymes, suggesting that these enzymes can track the growing ends of the filaments.

Septal localization and intracellular signaling

The formation of the Z-ring closely coincides with cellular processes associated with replication. Z-ring
formation coincides with the termination of genome replication in E. coli and 70% of chromosomal replication
in B. subtilis.[24] The timing of Z-ring formation suggests the possibility of a spatial or temporal signal that
permits the formation of FtsZ filaments. In Escherichia coli, at least two negative regulators of FtsZ assembly
form a bipolar gradient, such that the critical concentration of FtsZ required for FtsZ assembly is lowest at mid-
cell between the two segregating chromosomes. This type of regulation seems to occur in other species such as
Bacillus subtilis and Caulobacter crescentus. However, other species including Streptococcus pneumoniae and
Myxococcus xanthus seem to use positive regulators that stimulate FtsZ assembly at mid-cell.[25]

Communicating distress

FtsZ polymerization is also linked to stressors like DNA damage. DNA damage induces a variety of proteins
to be manufactured, one of them called SulA.[26] SulA prevents the polymerization and GTPase activity of
FtsZ. SulA accomplishes this task by binding to self-recognizing FtsZ sites. By sequestering FtsZ, the cell can
directly link DNA damage to inhibiting cell division.[27]

Preventing DNA damage

Like SulA, there are other mechanisms that prevent cell division that would result in disrupted genetic
information sent to daughter cells. So far, two proteins have been identified in E. coli and B. subtilis that
prevent division over the nucleoid region: Noc and SlmA. Noc gene knockouts result in cells that divide
without respect to the nucleoid region, resulting in its asymmetrical partitioning between the daughter cells.
The mechanism is not well understood, but thought to involve sequestration of FtsZ, preventing
polymerization over the nucleoid region.[28] The mechanism used by SlmA to inhibit FtsZ polymerization
over the nucleoid [29] is better understood, and uses two separate steps. One domain of SlmA binds to a FtsZ
polymer, then a separate domain of SlmA severs the polymer [30]. A similar mechanism is thought to be used
by MinC, another inhibitor of FtsZ polymerization involved in positioning of the FtsZ ring.[31]

Clinical significance
The number of multidrug-resistant bacterial strains is currently increasing; thus, the determination of drug
targets for the development of novel antimicrobial drugs is urgently needed. The potential role of FtsZ in the
blockage of cell division, together with its high degree of conservation across bacterial species, makes FtsZ a
highly attractive target for developing novel antibiotics.[32] Researchers have been working on synthetic
molecules and natural products as inhibitors of FtsZ.[33]

See also
Fission (biology)
Divisome

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