Difference between revisions of "FtsZ"

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(→‎FtsZ as antibacterial drug target)
(→‎FtsZ as antibacterial drug target)
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==FtsZ as antibacterial drug target==
 
==FtsZ as antibacterial drug target==
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<pubmed> 19583568 20410587 ,16174771, 20212044 20615583 21276094 23841620 </pubmed>
+
<pubmed> 19583568 20410587 ,16174771, 20212044 20615583 21276094 23841620 23855511 </pubmed>
  
 
==Other original Publications==
 
==Other original Publications==
 
<pubmed> 15288790, 15317782,12180929, 9364910,10323866, 19212404,15942012, 12007411,16420366, 16159787,10747015, 16950129, 16796675,10322023, 9495766,9287012,1569582,10878122, 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 </pubmed>
 
<pubmed> 15288790, 15317782,12180929, 9364910,10323866, 19212404,15942012, 12007411,16420366, 16159787,10747015, 16950129, 16796675,10322023, 9495766,9287012,1569582,10878122, 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 </pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 16:55, 19 July 2013

  • 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:
  • 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
    • 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

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:

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Reviews


FtsZ as antibacterial drug target


Other original Publications

David Ballesteros-Plaza, Isabel Holguera, Dirk-Jan Scheffers, Margarita Salas, Daniel Muñoz-Espín
Phage 29 phi protein p1 promotes replication by associating with the FtsZ ring of the divisome in Bacillus subtilis.
Proc Natl Acad Sci U S A: 2013, 110(30);12313-8
[PubMed:23836667] [WorldCat.org] [DOI] (I p)

Erik Nico Trip, Jan-Willem Veening, Eric J Stewart, Jeff Errington, Dirk-Jan Scheffers
Balanced transcription of cell division genes in Bacillus subtilis as revealed by single cell analysis.
Environ Microbiol: 2013, 15(12);3196-209
[PubMed:23701187] [WorldCat.org] [DOI] (I p)

P J Buske, Petra Anne Levin
A flexible C-terminal linker is required for proper FtsZ assembly in vitro and cytokinetic ring formation in vivo.
Mol Microbiol: 2013, 89(2);249-63
[PubMed:23692518] [WorldCat.org] [DOI] (I p)

Valdir Blasios, Alexandre W Bisson-Filho, Patricia Castellen, Maria Luiza C Nogueira, Jefferson Bettini, Rodrigo V Portugal, Ana Carolina M Zeri, Frederico J Gueiros-Filho
Genetic and biochemical characterization of the MinC-FtsZ interaction in Bacillus subtilis.
PLoS One: 2013, 8(4);e60690
[PubMed:23577149] [WorldCat.org] [DOI] (I p)

Michael P Strauss, Andrew T F Liew, Lynne Turnbull, Cynthia B Whitchurch, Leigh G Monahan, Elizabeth J Harry
3D-SIM super resolution microscopy reveals a bead-like arrangement for FtsZ and the division machinery: implications for triggering cytokinesis.
PLoS Biol: 2012, 10(9);e1001389
[PubMed:22984350] [WorldCat.org] [DOI] (I p)

An-Chun Chien, Shannon Kian Gharabiklou Zareh, Yan Mei Wang, Petra Anne Levin
Changes in the oligomerization potential of the division inhibitor UgtP co-ordinate Bacillus subtilis cell size with nutrient availability.
Mol Microbiol: 2012, 86(3);594-610
[PubMed:22931116] [WorldCat.org] [DOI] (I p)

Ewa Cendrowicz, Sebastiaan P van Kessel, Laura S van Bezouwen, Neeraj Kumar, Egbert J Boekema, Dirk-Jan Scheffers
Bacillus subtilis SepF binds to the C-terminus of FtsZ.
PLoS One: 2012, 7(8);e43293
[PubMed:22912848] [WorldCat.org] [DOI] (I p)

Jennifer K Wagner-Herman, Remi Bernard, Roisin Dunne, Alexandre W Bisson-Filho, Krithika Kumar, Trang Nguyen, Lawrence Mulcahy, John Koullias, Frederico J Gueiros-Filho, David Z Rudner
RefZ facilitates the switch from medial to polar division during spore formation in Bacillus subtilis.
J Bacteriol: 2012, 194(17);4608-18
[PubMed:22730127] [WorldCat.org] [DOI] (I p)

Christopher D A Rodrigues, Elizabeth J Harry
The Min system and nucleoid occlusion are not required for identifying the division site in Bacillus subtilis but ensure its efficient utilization.
PLoS Genet: 2012, 8(3);e1002561
[PubMed:22457634] [WorldCat.org] [DOI] (I p)

Paul J Buske, Petra Anne Levin
Extreme C terminus of bacterial cytoskeletal protein FtsZ plays fundamental role in assembly independent of modulatory proteins.
J Biol Chem: 2012, 287(14);10945-57
[PubMed:22298780] [WorldCat.org] [DOI] (I p)

Muhammet E Gündoğdu, Yoshikazu Kawai, Nada Pavlendova, Naotake Ogasawara, Jeff Errington, Dirk-Jan Scheffers, Leendert W Hamoen
Large ring polymers align FtsZ polymers for normal septum formation.
EMBO J: 2011, 30(3);617-26
[PubMed:21224850] [WorldCat.org] [DOI] (I p)

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)

Rut Carballido-López, Alex Formstone, Ying Li, S Dusko Ehrlich, Philippe Noirot, Jeff Errington
Actin homolog MreBH governs cell morphogenesis by localization of the cell wall hydrolase LytE.
Dev Cell: 2006, 11(3);399-409
[PubMed:16950129] [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)

Richard B Weart, Shunji Nakano, Brooke E Lane, Peter Zuber, Petra Anne Levin
The ClpX chaperone modulates assembly of the tubulin-like protein FtsZ.
Mol Microbiol: 2005, 57(1);238-49
[PubMed:15948963] [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)

Richard B Weart, Petra Anne Levin
Growth rate-dependent regulation of medial FtsZ ring formation.
J Bacteriol: 2003, 185(9);2826-34
[PubMed:12700262] [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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