Difference between revisions of "FtsZ"
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==FtsZ as antibacterial drug target== | ==FtsZ as antibacterial drug target== | ||
− | <pubmed> 19583568 20410587 ,16174771, 20212044 20615583 21276094 23841620 23855511 24079270 </pubmed> | + | <pubmed> 19583568 20410587 ,16174771, 20212044 20615583 21276094 23841620 23855511 24079270 24749867 </pubmed> |
==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 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 10:32, 24 April 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 This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
cell division, essential genes, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU15290
Phenotypes of a mutant
essential PubMed
Database entries
- BsubCyc: BSU15290
- 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
- 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
- BsubCyc: BSU15290
- UniProt: P17865
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulatory mechanism:
- Additional information:
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:
- Antibody: available in the Jeff Errington lab
Labs working on this gene/protein
- Imrich Barak, Slovak Academy of Science, Bratislava, Slovakia homepage
- Leendert Hamoen, CBCB, Newcastle University, UK
Your additional remarks
References
Reviews
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