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Literature summary for 3.6.5.6 extracted from
- GTPase activity-coupled treadmilling of the bacterial tubulin FtsZ organizes septal cell wall synthesis (2017), Science, 355, 744-747 .
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D158A | site-directed mutagenesis, altered directional movement of FtsI and septal PG composition in FtsZmut cells | Escherichia coli |
| D212G | site-directed mutagenesis, altered directional movement of FtsI and septal PG composition in FtsZmut cells | Escherichia coli |
| D269A | site-directed mutagenesis | Escherichia coli |
| E238A | site-directed mutagenesis | Escherichia coli |
| E250A | site-directed mutagenesis, altered directional movement of FtsI and septal PG composition in FtsZmut cells | Escherichia coli |
| G105S | site-directed mutagenesis | Escherichia coli |
| additional information | comparison of threadmilling speed and catalytic activity of wild-type and mutant cells and FtsZ polymers, overview. FtsZ GTPase mutants change the spatial distribution pattern but not the rate of septal PG synthesis | Escherichia coli |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytosol | - |
Escherichia coli | 5829 | - |
| inner membrane | during division, FtsZ polymerizes on the cytoplasmic face of the inner membrane to form a ring-like structure, the Z-ring, and recruits more than 30 proteins to the division site | Escherichia coli | - |
- |
| microtubule | - |
Escherichia coli | 5874 | - |
| additional information | FtsZ polymers exhibit apparently transverse, processive movement across the short axis of the cell, particularly in shorter cells | Escherichia coli | - |
- |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| GTP + H2O | Escherichia coli | - |
GDP + phosphate | - |
? |  |
| GTP + H2O | Escherichia coli BW25113 | - |
GDP + phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P0A9A6 | - |
- |
| Escherichia coli BW25113 | P0A9A6 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| GTP + H2O | - |
Escherichia coli | GDP + phosphate | - |
? | |
| GTP + H2O | - |
Escherichia coli BW25113 | GDP + phosphate | - |
? | |
| additional information | the guanosine triphosphatase (GTPase) activity of FtsZ is highly conserved, and the binding and hydrolysis of GTP underlie the dynamic assembly and disassembly of FtsZ | Escherichia coli | ? | - |
- |
|
| additional information | the guanosine triphosphatase (GTPase) activity of FtsZ is highly conserved, and the binding and hydrolysis of GTP underlie the dynamic assembly and disassembly of FtsZ | Escherichia coli BW25113 | ? | - |
- |
|
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| cell division protein | - |
Escherichia coli |
| GTPase | - |
Escherichia coli |
| guanosine triphosphatase | - |
Escherichia coli |
| tubulin FtsZ | - |
Escherichia coli |
| tubulin homolog FtsZ | - |
Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | in FtsZ mutants with severely reduced treadmilling, the spatial distribution of septal synthesis and the molecular composition and ultrastructure of the septal cell wall are substantially altered. Z-ring dynamics are significantly reduced in mutants with lower GTPase activity. In addition, the subunit exchange rate constants (kex) of these mutants decreases with kcat in a manner consistent with coupling to GTP hydrolysis. FtsZ GTPase mutants change the spatial distribution pattern but not the rate of septal PG synthesis | Escherichia coli |
| additional information | determination of Z-ring dynamics in live Escherichia coli strain BW25113 cells by using total internal reflection fluorescence (TIRF) microscopy to monitor the fluorescence of an FtsZ-GFP fusion protein. Mutants lacking one of the proteins that regulates the Z-ring (SlmA, SulA, MinC, ClpX, and ClpP) or stabilizes it (ZapA, ZapB, ZapC, ZapD, and MatP) also display wild-type Z-ring behavior. Thus, Z-ring dynamics are likely due to FtsZ's intrinsic polymerization properties, which are related to its GTPase activity. Z-ring dynamics were significantly reduced in mutants with lower GTPase activity | Escherichia coli |
| physiological function | the tubulin homologue FtsZ is the central component of the cell division machinery in nearly all walled bacterial species. During division, FtsZ polymerizes on the cytoplasmic face of the inner membrane to form a ring-like structure, the Z-ring, and recruits more than 30 proteins to the division site. Many of these proteins are involved in septal synthesis of the peptidoglycan (PG) cell wall. The guanosine triphosphatase (GTPase) activity of FtsZ is highly conserved, and the binding and hydrolysis of GTP underlie the dynamic assembly and disassembly of FtsZ. Exceptionally, in Escherichia coli the GTPase activity of FtsZ appears nonessential for cell division and does not dictate the cell constriction rate. In Escherichia coli cells, FtsZ exhibits dynamic treadmilling predominantly determined by its guanosine triphosphatase activity. The treadmilling dynamics direct the processive movement of the septal cell wall synthesis machinery but do not limit the rate of septal synthesis. FtsZ treadmilling provides a mechanism for achieving uniform septal cell wall synthesis to enable correct polar morphology | Escherichia coli |
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