Difference between revisions of "FtsZ"

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** interaction with [[UgtP]] inhibits [[FtsZ]] filament formation {{PubMed|22931116}}
 
** interaction with [[UgtP]] inhibits [[FtsZ]] filament formation {{PubMed|22931116}}
 
** FtsZ polymerization is inhibited by interaction with [[MinC]] {{PubMed|23577149}}
 
** FtsZ polymerization is inhibited by interaction with [[MinC]] {{PubMed|23577149}}
 +
** Z ring formation requires [[PdhA]] in a pyruvate-dependent manner {{PubMed|24825009}}
  
 
* '''[[SubtInteract|Interactions]]:'''  
 
* '''[[SubtInteract|Interactions]]:'''  
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==Other original Publications==
 
==Other original Publications==
−
<pubmed> 24007276 15288790, 15317782,12180929, 9364910,10323866, 19212404,15942012, 12007411,16420366, 16159787,10747015, 16950129, 16796675,10322023, 9495766,9287012,1569582,10878122, 17718511 11395470, 10449747, 17662947, 12368265,18284588,8600030,18588879,7592498, 19136590 , 19429628, 19141479 19843223 16484179 20199598 20566861 20711458 20807205 20933427 15948963 12700262 22298780 22457634 22730127 22984350 23577149 22931116,22912848,21224850 23692518 23701187 23836667 16159787 24300445 24316672 </pubmed>
+
<pubmed> 24007276 15288790, 15317782,12180929, 9364910,10323866, 19212404,15942012, 12007411,16420366, 16159787,10747015, 16950129, 16796675,10322023, 9495766,9287012,1569582,10878122, 17718511 11395470, 10449747, 17662947, 12368265,18284588,8600030,18588879,7592498, 19136590 , 19429628, 19141479 19843223 16484179 20199598 20566861 20711458 20807205 20933427 15948963 12700262 22298780 22457634 22730127 22984350 23577149 22931116,22912848,21224850 23692518 23701187 23836667 16159787 24300445 24316672 24825009</pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 17:33, 16 May 2014

  • Description: cell-division initiation protein (septum formation)

Gene name ftsZ
Synonyms ts-1
Essential yes PubMed
Product cell-division initiation protein (septum formation)
Function formation of Z-ring
Gene expression levels in SubtiExpress: ftsZ
Interactions involving this protein in SubtInteract: FtsZ
MW, pI 40 kDa, 4.814
Gene length, protein length 1146 bp, 382 aa
Immediate neighbours ftsA, bpr
Sequences Protein DNA DNA_with_flanks
Genetic context
FtsZ context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
FtsZ expression.png















Categories containing this gene/protein

cell division, essential genes, membrane proteins

This gene is a member of the following regulons

SigH regulon, WalR regulon

The gene

Basic information

  • Locus tag: BSU15290

Phenotypes of a mutant

essential PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: ftsZ family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:
    • Z ring formation is inhibited upon binding of MciZ to FtsZ
    • bundling of FtsZ protofilaments into strikingly long and regular tubular structures reminiscent of eukaryotic microtubules requires the prior formation of large ring polymers of SepF PubMed
    • interaction with UgtP inhibits FtsZ filament formation PubMed
    • FtsZ polymerization is inhibited by interaction with MinC PubMed
    • Z ring formation requires PdhA in a pyruvate-dependent manner PubMed
  • Localization:
    • septal at the cell membrane PubMed
    • septal localization partially depends on the proton motive force PubMed
    • Noc and the Min system ensure the efficient utilization of the division site at midcell in by ensuring Z ring placement PubMed
    • FtsZ is anchored to the cell membrane by either FtsA or SepF PubMed

Database entries

  • Structure: 2VAM, 2RHL (dimer with GDP)
  • KEGG entry: [3]
  • E.C. number:

Additional information

    • the novel antibiotic ADEP (acyldepsipeptides) causes FtsZ degradation via dysregulation ClpP activity (activity occurs even in the absence of an ATPase subunit (ClpC, ClpE, or ClpX)) PubMed

Expression and regulation

  • Regulatory mechanism:
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 2347 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 4359 PubMed

Biological materials

  • Mutant:
  • strains:
    • GP1372 (Pxyl ftsZ aphA3) disA::tet cdaS::ermC for xylose inducible expression of ftsZ, available in Jörg Stülke's lab
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Leigh G Monahan, Andrew T F Liew, Amy L Bottomley, Elizabeth J Harry
Division site positioning in bacteria: one size does not fit all.
Front Microbiol: 2014, 5;19
[PubMed:24550892] [WorldCat.org] [DOI] (P e)

An-Chun Chien, Norbert S Hill, Petra Anne Levin
Cell size control in bacteria.
Curr Biol: 2012, 22(9);R340-9
[PubMed:22575476] [WorldCat.org] [DOI] (I p)

Christine Kaimer, Peter L Graumann
Players between the worlds: multifunctional DNA translocases.
Curr Opin Microbiol: 2011, 14(6);719-25
[PubMed:22047950] [WorldCat.org] [DOI] (I p)

Clare L Kirkpatrick, Patrick H Viollier
New(s) to the (Z-)ring.
Curr Opin Microbiol: 2011, 14(6);691-7
[PubMed:21981908] [WorldCat.org] [DOI] (I p)

Harold P Erickson, David E Anderson, Masaki Osawa
FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one.
Microbiol Mol Biol Rev: 2010, 74(4);504-28
[PubMed:21119015] [WorldCat.org] [DOI] (I p)

Matthew T Cabeen, Christine Jacobs-Wagner
The bacterial cytoskeleton.
Annu Rev Genet: 2010, 44;365-92
[PubMed:21047262] [WorldCat.org] [DOI] (I p)

Marc Bramkamp, Suey van Baarle
Division site selection in rod-shaped bacteria.
Curr Opin Microbiol: 2009, 12(6);683-8
[PubMed:19884039] [WorldCat.org] [DOI] (I p)

David W Adams, Jeff Errington
Bacterial cell division: assembly, maintenance and disassembly of the Z ring.
Nat Rev Microbiol: 2009, 7(9);642-53
[PubMed:19680248] [WorldCat.org] [DOI] (I p)

Peter L Graumann
Cytoskeletal elements in bacteria.
Annu Rev Microbiol: 2007, 61;589-618
[PubMed:17506674] [WorldCat.org] [DOI] (P p)

Linda A Amos, Fusinita van den Ent, Jan Löwe
Structural/functional homology between the bacterial and eukaryotic cytoskeletons.
Curr Opin Cell Biol: 2004, 16(1);24-31
[PubMed:15037301] [WorldCat.org] [DOI] (P p)


FtsZ as antibacterial drug target

Dipty Singh, Anusri Bhattacharya, Ankit Rai, Hemendra Pal Singh Dhaked, Divya Awasthi, Iwao Ojima, Dulal Panda
SB-RA-2001 inhibits bacterial proliferation by targeting FtsZ assembly.
Biochemistry: 2014, 53(18);2979-92
[PubMed:24749867] [WorldCat.org] [DOI] (I p)

Filipa Marcelo, Sonia Huecas, Laura B Ruiz-Ávila, F Javier Cañada, Almudena Perona, Ana Poveda, Sonsoles Martín-Santamaría, Antonio Morreale, Jesús Jiménez-Barbero, José M Andreu
Interactions of bacterial cell division protein FtsZ with C8-substituted guanine nucleotide inhibitors. A combined NMR, biochemical and molecular modeling perspective.
J Am Chem Soc: 2013, 135(44);16418-28
[PubMed:24079270] [WorldCat.org] [DOI] (I p)

Laura B Ruiz-Avila, Sonia Huecas, Marta Artola, Albert Vergoñós, Erney Ramírez-Aportela, Emilia Cercenado, Isabel Barasoain, Henar Vázquez-Villa, Mar Martín-Fontecha, Pablo Chacón, María L López-Rodríguez, José M Andreu
Synthetic inhibitors of bacterial cell division targeting the GTP-binding site of FtsZ.
ACS Chem Biol: 2013, 8(9);2072-83
[PubMed:23855511] [WorldCat.org] [DOI] (I p)

Anusri Bhattacharya, Bhavya Jindal, Parminder Singh, Anindya Datta, Dulal Panda
Plumbagin inhibits cytokinesis in Bacillus subtilis by inhibiting FtsZ assembly--a mechanistic study of its antibacterial activity.
FEBS J: 2013, 280(18);4585-99
[PubMed:23841620] [WorldCat.org] [DOI] (I p)

David W Adams, Ling Juan Wu, Lloyd G Czaplewski, Jeff Errington
Multiple effects of benzamide antibiotics on FtsZ function.
Mol Microbiol: 2011, 80(1);68-84
[PubMed:21276094] [WorldCat.org] [DOI] (I p)

Simranjeet Kaur, Niraj H Modi, Dulal Panda, Nilanjan Roy
Probing the binding site of curcumin in Escherichia coli and Bacillus subtilis FtsZ--a structural insight to unveil antibacterial activity of curcumin.
Eur J Med Chem: 2010, 45(9);4209-14
[PubMed:20615583] [WorldCat.org] [DOI] (I p)

Kumiko W Shimotohno, Fujio Kawamura, Yousuke Natori, Hideaki Nanamiya, Junji Magae, Hiromitsu Ogata, Toyoshige Endo, Takeshi Suzuki, Hiroshi Yamaki
Inhibition of septation in Bacillus subtilis by a peptide antibiotic, edeine B(1).
Biol Pharm Bull: 2010, 33(4);568-71
[PubMed:20410587] [WorldCat.org] [DOI] (I p)

José M Andreu, Claudia Schaffner-Barbero, Sonia Huecas, Dulce Alonso, María L Lopez-Rodriguez, Laura B Ruiz-Avila, Rafael Núñez-Ramírez, Oscar Llorca, Antonio J Martín-Galiano
The antibacterial cell division inhibitor PC190723 is an FtsZ polymer-stabilizing agent that induces filament assembly and condensation.
J Biol Chem: 2010, 285(19);14239-46
[PubMed:20212044] [WorldCat.org] [DOI] (I p)

Tushar K Beuria, Parminder Singh, Avadhesha Surolia, Dulal Panda
Promoting assembly and bundling of FtsZ as a strategy to inhibit bacterial cell division: a new approach for developing novel antibacterial drugs.
Biochem J: 2009, 423(1);61-9
[PubMed:19583568] [WorldCat.org] [DOI] (I e)

Neil R Stokes, Jörg Sievers, Stephanie Barker, James M Bennett, David R Brown, Ian Collins, Veronica M Errington, David Foulger, Michelle Hall, Rowena Halsey, Hazel Johnson, Valerie Rose, Helena B Thomaides, David J Haydon, Lloyd G Czaplewski, Jeff Errington
Novel inhibitors of bacterial cytokinesis identified by a cell-based antibiotic screening assay.
J Biol Chem: 2005, 280(48);39709-15
[PubMed:16174771] [WorldCat.org] [DOI] (P p)


Other original Publications

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