Difference between revisions of "TasA"

From SubtiWiki
Jump to: navigation, search
(Biological materials)
Line 139: Line 139:
 
* '''Mutant:'''
 
* '''Mutant:'''
 
** 1S121 ( ''tasA''::''spec''), {{PubMed|10049401}}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1S121&Search=1S121 BGSC]
 
** 1S121 ( ''tasA''::''spec''), {{PubMed|10049401}}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1S121&Search=1S121 BGSC]
 +
** GP1672 (''sinR-tasA''::''cat''), available in [[Stülke]] lab
 +
** GP1663 (''yghG-sinI-sinR-tasA''), available in [[Stülke]] lab
  
 
* '''Expression vector:'''
 
* '''Expression vector:'''

Revision as of 13:28, 1 November 2013

  • Description: major component of biofilm matrix, forms amyloid fibers

Gene name tasA
Synonyms cotN, yqhF
Essential no
Product major component of biofilm matrix
Function biofilm formation
Gene expression levels in SubtiExpress: tasA
Interactions involving this protein in SubtInteract: TasA
Regulation of this protein in SubtiPathways:
Biofilm, Protein secretion
MW, pI 28 kDa, 5.442
Gene length, protein length 783 bp, 261 aa
Immediate neighbours sinR, sipW
Sequences Protein DNA DNA_with_flanks
Genetic context
TasA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
TasA expression.png















Categories containing this gene/protein

biofilm formation

This gene is a member of the following regulons

AbrB regulon, RemA regulon, SinR regulon

The gene

Basic information

  • Locus tag: BSU24620

Phenotypes of a mutant

  • altered cell death pattern in colonies PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: forms amyloid fibers that bind cells together in the biofilm PubMed
  • Protein family: peptidase M73 family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Additional information:

Biological materials

  • Mutant:
    • 1S121 ( tasA::spec), PubMed, available at BGSC
    • GP1672 (sinR-tasA::cat), available in Stülke lab
    • GP1663 (yghG-sinI-sinR-tasA), available in Stülke lab
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Adam Driks
Tapping into the biofilm: insights into assembly and disassembly of a novel amyloid fibre in Bacillus subtilis.
Mol Microbiol: 2011, 80(5);1133-6
[PubMed:21488983] [WorldCat.org] [DOI] (I p)

Massimiliano Marvasi, Pieter T Visscher, Lilliam Casillas Martinez
Exopolymeric substances (EPS) from Bacillus subtilis: polymers and genes encoding their synthesis.
FEMS Microbiol Lett: 2010, 313(1);1-9
[PubMed:20735481] [WorldCat.org] [DOI] (I p)

Yunrong Chai, Thomas Norman, Roberto Kolter, Richard Losick
An epigenetic switch governing daughter cell separation in Bacillus subtilis.
Genes Dev: 2010, 24(8);754-65
[PubMed:20351052] [WorldCat.org] [DOI] (I p)


Original publications

Jared T Winkelman, Anna C Bree, Ashley R Bate, Patrick Eichenberger, Richard L Gourse, Daniel B Kearns
RemA is a DNA-binding protein that activates biofilm matrix gene expression in Bacillus subtilis.
Mol Microbiol: 2013, 88(5);984-97
[PubMed:23646920] [WorldCat.org] [DOI] (I p)

Liraz Chai, Diego Romero, Can Kayatekin, Barak Akabayov, Hera Vlamakis, Richard Losick, Roberto Kolter
Isolation, characterization, and aggregation of a structured bacterial matrix precursor.
J Biol Chem: 2013, 288(24);17559-68
[PubMed:23632024] [WorldCat.org] [DOI] (I p)

Diego Romero, Edgardo Sanabria-Valentín, Hera Vlamakis, Roberto Kolter
Biofilm inhibitors that target amyloid proteins.
Chem Biol: 2013, 20(1);102-10
[PubMed:23352144] [WorldCat.org] [DOI] (I p)

Emma K Andersson, Matthew Chapman
Small molecule disruption of B. subtilis biofilms by targeting the amyloid matrix.
Chem Biol: 2013, 20(1);5-7
[PubMed:23352134] [WorldCat.org] [DOI] (I p)

Munehiro Asally, Mark Kittisopikul, Pau Rué, Yingjie Du, Zhenxing Hu, Tolga Çağatay, Andra B Robinson, Hongbing Lu, Jordi Garcia-Ojalvo, Gürol M Süel
Localized cell death focuses mechanical forces during 3D patterning in a biofilm.
Proc Natl Acad Sci U S A: 2012, 109(46);18891-6
[PubMed:23012477] [WorldCat.org] [DOI] (I p)

Christine Diethmaier, Nico Pietack, Katrin Gunka, Christoph Wrede, Martin Lehnik-Habrink, Christina Herzberg, Sebastian Hübner, Jörg Stülke
A novel factor controlling bistability in Bacillus subtilis: the YmdB protein affects flagellin expression and biofilm formation.
J Bacteriol: 2011, 193(21);5997-6007
[PubMed:21856853] [WorldCat.org] [DOI] (I p)

Martin Lehnik-Habrink, Marc Schaffer, Ulrike Mäder, Christine Diethmaier, Christina Herzberg, Jörg Stülke
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y.
Mol Microbiol: 2011, 81(6);1459-73
[PubMed:21815947] [WorldCat.org] [DOI] (I p)

Diego Romero, Claudio Aguilar, Richard Losick, Roberto Kolter
Amyloid fibers provide structural integrity to Bacillus subtilis biofilms.
Proc Natl Acad Sci U S A: 2010, 107(5);2230-4
[PubMed:20080671] [WorldCat.org] [DOI] (I p)

Birgit Voigt, Haike Antelmann, Dirk Albrecht, Armin Ehrenreich, Karl-Heinz Maurer, Stefan Evers, Gerhard Gottschalk, Jan Maarten van Dijl, Thomas Schweder, Michael Hecker
Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis.
J Mol Microbiol Biotechnol: 2009, 16(1-2);53-68
[PubMed:18957862] [WorldCat.org] [DOI] (I p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

Kazuo Kobayashi
SlrR/SlrA controls the initiation of biofilm formation in Bacillus subtilis.
Mol Microbiol: 2008, 69(6);1399-410
[PubMed:18647168] [WorldCat.org] [DOI] (I p)

Frances Chu, Daniel B Kearns, Anna McLoon, Yunrong Chai, Roberto Kolter, Richard Losick
A novel regulatory protein governing biofilm formation in Bacillus subtilis.
Mol Microbiol: 2008, 68(5);1117-27
[PubMed:18430133] [WorldCat.org] [DOI] (I p)

Yunrong Chai, Frances Chu, Roberto Kolter, Richard Losick
Bistability and biofilm formation in Bacillus subtilis.
Mol Microbiol: 2008, 67(2);254-63
[PubMed:18047568] [WorldCat.org] [DOI] (P p)

Mark A Strauch, Benjamin G Bobay, John Cavanagh, Fude Yao, Angelo Wilson, Yoann Le Breton
Abh and AbrB control of Bacillus subtilis antimicrobial gene expression.
J Bacteriol: 2007, 189(21);7720-32
[PubMed:17720793] [WorldCat.org] [DOI] (P p)

Steven S Branda, Frances Chu, Daniel B Kearns, Richard Losick, Roberto Kolter
A major protein component of the Bacillus subtilis biofilm matrix.
Mol Microbiol: 2006, 59(4);1229-38
[PubMed:16430696] [WorldCat.org] [DOI] (P p)

Frances Chu, Daniel B Kearns, Steven S Branda, Roberto Kolter, Richard Losick
Targets of the master regulator of biofilm formation in Bacillus subtilis.
Mol Microbiol: 2006, 59(4);1216-28
[PubMed:16430695] [WorldCat.org] [DOI] (P p)

Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147] [WorldCat.org] [DOI] (P p)

A G Stöver, A Driks
Regulation of synthesis of the Bacillus subtilis transition-phase, spore-associated antibacterial protein TasA.
J Bacteriol: 1999, 181(17);5476-81
[PubMed:10464223] [WorldCat.org] [DOI] (P p)

M Serrano, R Zilhão, E Ricca, A J Ozin, C P Moran, A O Henriques
A Bacillus subtilis secreted protein with a role in endospore coat assembly and function.
J Bacteriol: 1999, 181(12);3632-43
[PubMed:10368135] [WorldCat.org] [DOI] (P p)

A G Stöver, A Driks
Secretion, localization, and antibacterial activity of TasA, a Bacillus subtilis spore-associated protein.
J Bacteriol: 1999, 181(5);1664-72
[PubMed:10049401] [WorldCat.org] [DOI] (P p)