Difference between revisions of "FtsZ"

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(→‎FtsZ as antibacterial drug target)
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=== Additional information===
 
=== Additional information===
−
 
−
 
−
 
  
 
=The protein=
 
=The protein=
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* '''Cofactor(s):'''
 
* '''Cofactor(s):'''
  
−
* '''Effectors of protein activity:''' Z ring formation is inhibited upon binding of [[MciZ]] to FtsZ
+
* '''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|21224850}}
  
−
* '''Interactions:''' [[FtsZ]]-[[ZapA]] {{PubMed|19843223}}, [[FtsZ]]-[[EzrA]] {{PubMed|10449747}},  [[FtsZ]]-[[SpoIIE]],  [[FtsZ]]-[[FtsA]],  [[FtsZ]]-[[FtsZ]] {{PubMed|17662947}},  [[MciZ]]-[[FtsZ]] {{PubMed|18284588}}, [[FtsZ]]-[[SepF]]
+
* '''Interactions:'''  
 +
** [[FtsZ]]-[[ZapA]] {{PubMed|19843223}}
 +
** [[FtsZ]]-[[EzrA]] {{PubMed|10449747}}
 +
** [[FtsZ]]-[[SpoIIE]]
 +
** [[FtsZ]]-[[FtsA]]
 +
** [[FtsZ]]-[[FtsZ]] {{PubMed|17662947}}
 +
** [[MciZ]]-[[FtsZ]] {{PubMed|18284588}}
 +
** [[FtsZ]]-[[SepF]] {{PubMed|16420366}}
  
 
* '''Localization:'''  
 
* '''Localization:'''  
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==Other original Publications==
 
==Other original Publications==
 +
'''Additional publications:''' {{PubMed|21224850}}
 
<pubmed> 15288790, 15317782,12180929, 9364910,10323866, 19212404,15942012, 12007411,16420366, 16159787,10747015, 16796675,10322023,9495766,9287012,1569582,10878122,11395470,10449747,17662947,12368265,18284588,8600030,18588879,7592498, 19136590 , 19429628, 19141479 19843223 16484179 20199598 20566861 20711458 20807205 20933427 </pubmed>
 
<pubmed> 15288790, 15317782,12180929, 9364910,10323866, 19212404,15942012, 12007411,16420366, 16159787,10747015, 16796675,10322023,9495766,9287012,1569582,10878122,11395470,10449747,17662947,12368265,18284588,8600030,18588879,7592498, 19136590 , 19429628, 19141479 19843223 16484179 20199598 20566861 20711458 20807205 20933427 </pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 11:48, 19 February 2011

  • 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
MW, pI 40 kDa, 4.814
Gene length, protein length 1146 bp, 382 aa
Immediate neighbours ftsA, bpr
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
FtsZ context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

cell division, essential genes, membrane proteins

This gene is a member of the following regulons

AbrB regulon, 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:
  • Domains:
  • Modification:
  • Cofactor(s):
  • 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
  • Localization:
    • septal at the cell membrane PubMed
    • septal localization partially depends on the proton motive force PubMed

Database entries

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

Additional information

Expression and regulation

  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:

Labs working on this gene/protein

Imrich Barak, Slovak Academy of Science, Bratislava, Slovakia homepage

Your additional remarks

References

Reviews

Additional reviews: PubMed

FtsZ as antibacterial drug target

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

Additional publications: PubMed

Phoebe C Jennings, Guy C Cox, Leigh G Monahan, Elizabeth J Harry
Super-resolution imaging of the bacterial cytokinetic protein FtsZ.
Micron: 2011, 42(4);336-41
[PubMed:20933427] [WorldCat.org] [DOI] (I p)

Remi Bernard, Kathleen A Marquis, David Z Rudner
Nucleoid occlusion prevents cell division during replication fork arrest in Bacillus subtilis.
Mol Microbiol: 2010, 78(4);866-82
[PubMed:20807205] [WorldCat.org] [DOI] (I p)

Inês Filipa Fernandes de Oliveira, Anabela de Sousa Borges, Viola Kooij, Jeremy Bartosiak-Jentys, Joen Luirink, Dirk-Jan Scheffers
Characterization of ftsZ mutations that render Bacillus subtilis resistant to MinC.
PLoS One: 2010, 5(8);e12048
[PubMed:20711458] [WorldCat.org] [DOI] (I e)

Henrik Strahl, Leendert W Hamoen
Membrane potential is important for bacterial cell division.
Proc Natl Acad Sci U S A: 2010, 107(27);12281-6
[PubMed:20566861] [WorldCat.org] [DOI] (I p)

S Moriya, R A Rashid, C D Andrade Rodrigues, E J Harry
Influence of the nucleoid and the early stages of DNA replication on positioning the division site in Bacillus subtilis.
Mol Microbiol: 2010, 76(3);634-47
[PubMed:20199598] [WorldCat.org] [DOI] (I p)

Leigh G Monahan, Andrew Robinson, Elizabeth J Harry
Lateral FtsZ association and the assembly of the cytokinetic Z ring in bacteria.
Mol Microbiol: 2009, 74(4);1004-17
[PubMed:19843223] [WorldCat.org] [DOI] (I p)

Pamela Gamba, Jan-Willem Veening, Nigel J Saunders, Leendert W Hamoen, Richard A Daniel
Two-step assembly dynamics of the Bacillus subtilis divisome.
J Bacteriol: 2009, 191(13);4186-94
[PubMed:19429628] [WorldCat.org] [DOI] (I p)

M Leaver, P Domínguez-Cuevas, J M Coxhead, R A Daniel, J Errington
Life without a wall or division machine in Bacillus subtilis.
Nature: 2009, 457(7231);849-53
[PubMed:19212404] [WorldCat.org] [DOI] (I p)

James A Gregory, Eric C Becker, Kit Pogliano
Bacillus subtilis MinC destabilizes FtsZ-rings at new cell poles and contributes to the timing of cell division.
Genes Dev: 2008, 22(24);3475-88
[PubMed:19141479] [WorldCat.org] [DOI] (P p)

Daniel P Haeusser, Amy H Lee, Richard B Weart, Petra Anne Levin
ClpX inhibits FtsZ assembly in a manner that does not require its ATP hydrolysis-dependent chaperone activity.
J Bacteriol: 2009, 191(6);1986-91
[PubMed:19136590] [WorldCat.org] [DOI] (I p)

Dirk-Jan Scheffers
The effect of MinC on FtsZ polymerization is pH dependent and can be counteracted by ZapA.
FEBS Lett: 2008, 582(17);2601-8
[PubMed:18588879] [WorldCat.org] [DOI] (P p)

Aaron A Handler, Joo Eun Lim, Richard Losick
Peptide inhibitor of cytokinesis during sporulation in Bacillus subtilis.
Mol Microbiol: 2008, 68(3);588-99
[PubMed:18284588] [WorldCat.org] [DOI] (I p)

Richard B Weart, Amy H Lee, An-Chun Chien, Daniel P Haeusser, Norbert S Hill, Petra Anne Levin
A metabolic sensor governing cell size in bacteria.
Cell: 2007, 130(2);335-47
[PubMed:17662947] [WorldCat.org] [DOI] (P p)

Shu Ishikawa, Yoshikazu Kawai, Konosuke Hiramatsu, Masayoshi Kuwano, Naotake Ogasawara
A new FtsZ-interacting protein, YlmF, complements the activity of FtsA during progression of cell division in Bacillus subtilis.
Mol Microbiol: 2006, 60(6);1364-80
[PubMed:16796675] [WorldCat.org] [DOI] (P p)

Katherine A Michie, Leigh G Monahan, Peter L Beech, Elizabeth J Harry
Trapping of a spiral-like intermediate of the bacterial cytokinetic protein FtsZ.
J Bacteriol: 2006, 188(5);1680-90
[PubMed:16484179] [WorldCat.org] [DOI] (P p)

Leendert W Hamoen, Jean-Christophe Meile, Wouter de Jong, Philippe Noirot, Jeff Errington
SepF, a novel FtsZ-interacting protein required for a late step in cell division.
Mol Microbiol: 2006, 59(3);989-99
[PubMed:16420366] [WorldCat.org] [DOI] (P p)

S O Jensen, L S Thompson, E J Harry
Cell division in Bacillus subtilis: FtsZ and FtsA association is Z-ring independent, and FtsA is required for efficient midcell Z-Ring assembly.
J Bacteriol: 2005, 187(18);6536-44
[PubMed:16159787] [WorldCat.org] [DOI] (P p)

Andrea Feucht, Jeffery Errington
ftsZ mutations affecting cell division frequency, placement and morphology in Bacillus subtilis.
Microbiology (Reading): 2005, 151(Pt 6);2053-2064
[PubMed:15942012] [WorldCat.org] [DOI] (P p)

David E Anderson, Frederico J Gueiros-Filho, Harold P Erickson
Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins.
J Bacteriol: 2004, 186(17);5775-81
[PubMed:15317782] [WorldCat.org] [DOI] (P p)

Harry H Low, Martin C Moncrieffe, Jan Löwe
The crystal structure of ZapA and its modulation of FtsZ polymerisation.
J Mol Biol: 2004, 341(3);839-52
[PubMed:15288790] [WorldCat.org] [DOI] (P p)

Frederico J Gueiros-Filho, Richard Losick
A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ.
Genes Dev: 2002, 16(19);2544-56
[PubMed:12368265] [WorldCat.org] [DOI] (P p)

Andrea Feucht, Laura Abbotts, Jeffery Errington
The cell differentiation protein SpoIIE contains a regulatory site that controls its phosphatase activity in response to asymmetric septation.
Mol Microbiol: 2002, 45(4);1119-30
[PubMed:12180929] [WorldCat.org] [DOI] (P p)

Sigal Ben-Yehuda, Richard Losick
Asymmetric cell division in B. subtilis involves a spiral-like intermediate of the cytokinetic protein FtsZ.
Cell: 2002, 109(2);257-66
[PubMed:12007411] [WorldCat.org] [DOI] (P p)

P L Graumann, R Losick
Coupling of asymmetric division to polar placement of replication origin regions in Bacillus subtilis.
J Bacteriol: 2001, 183(13);4052-60
[PubMed:11395470] [WorldCat.org] [DOI] (P p)

Keisuke Fukuchi, Yasuhiro Kasahara, Kei Asai, Kazuo Kobayashi, Shigeki Moriya, Naotake Ogasawara
The essential two-component regulatory system encoded by yycF and yycG modulates expression of the ftsAZ operon in Bacillus subtilis.
Microbiology (Reading): 2000, 146 ( Pt 7);1573-1583
[PubMed:10878122] [WorldCat.org] [DOI] (P p)

I Lucet, A Feucht, M D Yudkin, J Errington
Direct interaction between the cell division protein FtsZ and the cell differentiation protein SpoIIE.
EMBO J: 2000, 19(7);1467-75
[PubMed:10747015] [WorldCat.org] [DOI] (P p)

P A Levin, I G Kurtser, A D Grossman
Identification and characterization of a negative regulator of FtsZ ring formation in Bacillus subtilis.
Proc Natl Acad Sci U S A: 1999, 96(17);9642-7
[PubMed:10449747] [WorldCat.org] [DOI] (P p)

N King, O Dreesen, P Stragier, K Pogliano, R Losick
Septation, dephosphorylation, and the activation of sigmaF during sporulation in Bacillus subtilis.
Genes Dev: 1999, 13(9);1156-67
[PubMed:10323866] [WorldCat.org] [DOI] (P p)

L B Pedersen, E R Angert, P Setlow
Septal localization of penicillin-binding protein 1 in Bacillus subtilis.
J Bacteriol: 1999, 181(10);3201-11
[PubMed:10322023] [WorldCat.org] [DOI] (P p)

A Khvorova, L Zhang, M L Higgins, P J Piggot
The spoIIE locus is involved in the Spo0A-dependent switch in the location of FtsZ rings in Bacillus subtilis.
J Bacteriol: 1998, 180(5);1256-60
[PubMed:9495766] [WorldCat.org] [DOI] (P p)

P A Levin, R Losick, P Stragier, F Arigoni
Localization of the sporulation protein SpoIIE in Bacillus subtilis is dependent upon the cell division protein FtsZ.
Mol Microbiol: 1997, 25(5);839-46
[PubMed:9364910] [WorldCat.org] [DOI] (P p)

X Wang, J Huang, A Mukherjee, C Cao, J Lutkenhaus
Analysis of the interaction of FtsZ with itself, GTP, and FtsA.
J Bacteriol: 1997, 179(17);5551-9
[PubMed:9287012] [WorldCat.org] [DOI] (P p)

P A Levin, R Losick
Transcription factor Spo0A switches the localization of the cell division protein FtsZ from a medial to a bipolar pattern in Bacillus subtilis.
Genes Dev: 1996, 10(4);478-88
[PubMed:8600030] [WorldCat.org] [DOI] (P p)

M A Strauch
Delineation of AbrB-binding sites on the Bacillus subtilis spo0H, kinB, ftsAZ, and pbpE promoters and use of a derived homology to identify a previously unsuspected binding site in the bsuB1 methylase promote.
J Bacteriol: 1995, 177(23);6999-7002
[PubMed:7592498] [WorldCat.org] [DOI] (P p)

G Gonzy-Tréboul, C Karmazyn-Campelli, P Stragier
Developmental regulation of transcription of the Bacillus subtilis ftsAZ operon.
J Mol Biol: 1992, 224(4);967-79
[PubMed:1569582] [WorldCat.org] [DOI] (P p)

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