TasA

• 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: tasA
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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

• BsubCyc: BSU24620

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Cofactors:

• Effectors of protein activity:

• Interactions:
  • forms fibers of variable length and 10-15 nm in width PubMed
  • TapA-TasA PubMed
  • SipW-TasA PubMed

• Localization:
  • extracellular (signal peptide) PubMed, secretion requires SipW PubMed
  • membrane PubMed

Database entries

• BsubCyc: BSU24620

• Structure:

• UniProt: P54507

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: tapA-sipW-tasA PubMed

• Expression browser: tasA PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • repressed by casamino acids PubMed
  • repressed by SinR PubMed
  • repressed during logrithmic growth (AbrB) PubMed

• Regulatory mechanism:
  • AbrB: transcription repression PubMed
  • SinR: transcription repression PubMed
  • RemA: transcription activation PubMed

• Additional information:
  • induction by sequestration of SinR by SinI or SlrA PubMed or by SlrR PubMed
  • the tapA-sipW-tasA operon is not expressed in a ymdB mutant PubMed
  • the amount of the mRNA is substantially decreased upon depletion of RNase Y (this is likely due to the increased stability of the sinR mRNA) PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 199 PubMed

Biological materials

• Mutants:
  • 1S121 (tasA::spec), PubMed, available at BGSC
  • GP1571 (cat), available in Jörg Stülke's lab
  • GP1663 (deletion of yqhG-sinI-sinR-tasA), available in Jörg Stülke's lab
  • GP1672 (deletion of sinR-tasA::cat) PubMed, available in Jörg Stülke's lab
  • GP1819 (aphA3), available in Jörg Stülke's lab

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Original publications

Diego Romero, Hera Vlamakis, Richard Losick, Roberto Kolter
Functional analysis of the accessory protein TapA in Bacillus subtilis amyloid fiber assembly.
J Bacteriol: 2014, 196(8);1505-13
[PubMed:24488317] [WorldCat.org] [DOI] (I p)

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)