AbrB

• Description: transcriptional regulator of transition state genes
  
  

Gene name	abrB
Synonyms	cpsX
Essential	no
Product	transcriptional regulator
Function	regulation of gene expression during the transition from growth to stationary phase
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism, Sugar catabolism
MW, pI	10 kDa, 6.57
Gene length, protein length	288 bp, 96 aa
Immediate neighbours	yabC, metS
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU00370

Phenotypes of a mutant

No swarming motility on B medium. PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s): Abh, SpoVT (only N-terminal domain)

Genes/ operons controlled by AbrB

• Activated by AbrB: citB, comK, hpr, rbsR-rbsK-rbsD-rbsA-rbsC-rbsB

• Repressed by AbrB: abrB, aprE, ftsA-ftsZ, kinC, motA, nprE, pbpE, spo0H, spoVG, spo0E, tycA, sbo-alb, yqxM-sipW-tasA

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity: interaction with AbbA results in inactivation of AbrB PubMed

• Interactions: AbrB-AbbA PubMed

• Localization:

Database entries

• Structure: 1Z0R (N-terminal DNA recognition domain), 1Z0R (N-terminal DNA recognition domain) NCBI PubMed

• Swiss prot entry: P08874

• KEGG entry: [3]

Expression and regulation

• Operon: abrB PubMed

• Sigma factor: SigA PubMed

• Regulation: expressed at the onset of stationary phase PubMed
  • repressed during logrithmic growth (AbrB) PubMed

• Regulatory mechanism: repressed by Spo0A-P PubMed
  • AbrB: transcription repression PubMed

• Additional information:

Biological materials

• Mutant: TT731 (aphA3)

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

Richard Losick, Harvard Univ., Cambridge, USA homepage

Mark Strauch, Baltimore, USA homepage

References

Yun Luo, John D Helmann
Extracytoplasmic function sigma factors with overlapping promoter specificity regulate sublancin production in Bacillus subtilis.
J Bacteriol: 2009, 191(15);4951-8
[PubMed:19465659] [WorldCat.org] [DOI] (I p)

Kassem Hamze, Daria Julkowska, Sabine Autret, Krzysztof Hinc, Krzysztofa Nagorska, Agnieszka Sekowska, I Barry Holland, Simone J Séror
Identification of genes required for different stages of dendritic swarming in Bacillus subtilis, with a novel role for phrC.
Microbiology (Reading): 2009, 155(Pt 2);398-412
[PubMed:19202088] [WorldCat.org] [DOI] (P p)

Allison V Banse, Arnaud Chastanet, Lilah Rahn-Lee, Errett C Hobbs, Richard Losick
Parallel pathways of repression and antirepression governing the transition to stationary phase in Bacillus subtilis.
Proc Natl Acad Sci U S A: 2008, 105(40);15547-52
[PubMed:18840696] [WorldCat.org] [DOI] (I 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)

Sina Jordan, Eva Rietkötter, Mark A Strauch, Falk Kalamorz, Bronwyn G Butcher, John D Helmann, Thorsten Mascher
LiaRS-dependent gene expression is embedded in transition state regulation in Bacillus subtilis.
Microbiology (Reading): 2007, 153(Pt 8);2530-2540
[PubMed:17660417] [WorldCat.org] [DOI] (P p)

Benjamin G Bobay, Geoffrey A Mueller, Richele J Thompson, Alexey G Murzin, Ronald A Venters, Mark A Strauch, John Cavanagh
NMR structure of AbhN and comparison with AbrBN: FIRST insights into the DNA binding promiscuity and specificity of AbrB-like transition state regulator proteins.
J Biol Chem: 2006, 281(30);21399-21409
[PubMed:16702211] [WorldCat.org] [DOI] (P p)

Benjamin G Bobay, Antonina Andreeva, Geoffrey A Mueller, John Cavanagh, Alexey G Murzin
Revised structure of the AbrB N-terminal domain unifies a diverse superfamily of putative DNA-binding proteins.
FEBS Lett: 2005, 579(25);5669-74
[PubMed:16223496] [WorldCat.org] [DOI] (P p)

Fude Yao, Mark A Strauch
Independent and interchangeable multimerization domains of the AbrB, Abh, and SpoVT global regulatory proteins.
J Bacteriol: 2005, 187(18);6354-62
[PubMed:16159768] [WorldCat.org] [DOI] (P p)

Benjamin G Bobay, Linda Benson, Stephen Naylor, Brett Feeney, A Clay Clark, Michael B Goshe, Mark A Strauch, Richele Thompson, John Cavanagh
Evaluation of the DNA binding tendencies of the transition state regulator AbrB.
Biochemistry: 2004, 43(51);16106-18
[PubMed:15610005] [WorldCat.org] [DOI] (P p)

Hyun-Jin Kim, Sam-In Kim, Manoja Ratnayake-Lecamwasam, Kiyoshi Tachikawa, Abraham L Sonenshein, Mark Strauch
Complex regulation of the Bacillus subtilis aconitase gene.
J Bacteriol: 2003, 185(5);1672-80
[PubMed:12591885] [WorldCat.org] [DOI] (P p)

Linda M Benson, Jeffrey L Vaughn, Mark A Strauch, Benjamin G Bobay, Richele Thompson, Stephen Naylor, John Cavanagh
Macromolecular assembly of the transition state regulator AbrB in its unbound and complexed states probed by microelectrospray ionization mass spectrometry.
Anal Biochem: 2002, 306(2);222-7
[PubMed:12123659] [WorldCat.org] [DOI] (P p)

Qiang Qian, Chien Y Lee, John D Helmann, Mark A Strauch
AbrB is a regulator of the sigma(W) regulon in Bacillus subtilis.
FEMS Microbiol Lett: 2002, 211(2);219-23
[PubMed:12076816] [WorldCat.org] [DOI] (P p)

Z E V Phillips, M A Strauch
Bacillus subtilis sporulation and stationary phase gene expression.
Cell Mol Life Sci: 2002, 59(3);392-402
[PubMed:11964117] [WorldCat.org] [DOI] (P p)

Sasha H Shafikhani, Ines Mandic-Mulec, Mark A Strauch, Issar Smith, Terrance Leighton
Postexponential regulation of sin operon expression in Bacillus subtilis.
J Bacteriol: 2002, 184(2);564-71
[PubMed:11751836] [WorldCat.org] [DOI] (P p)

Z E Phillips, M A Strauch
Role of Cys54 in AbrB multimerization and DNA-binding activity.
FEMS Microbiol Lett: 2001, 203(2);207-10
[PubMed:11583849] [WorldCat.org] [DOI] (P p)

K Xu, M A Strauch
DNA-binding activity of amino-terminal domains of the Bacillus subtilis AbrB protein.
J Bacteriol: 2001, 183(13);4094-8
[PubMed:11395475] [WorldCat.org] [DOI] (P p)

J L Vaughn, V Feher, S Naylor, M A Strauch, J Cavanagh
Novel DNA binding domain and genetic regulation model of Bacillus subtilis transition state regulator abrB.
Nat Struct Biol: 2000, 7(12);1139-46
[PubMed:11101897] [WorldCat.org] [DOI] (P p)

K Xu, D Clark, M A Strauch
Analysis of abrB mutations, mutant proteins, and why abrB does not utilize a perfect consensus in the -35 region of its sigma A promoter.
J Biol Chem: 1996, 271(5);2621-6
[PubMed:8576231] [WorldCat.org] [DOI] (P p)

K Xu, M A Strauch
In vitro selection of optimal AbrB-binding sites: comparison to known in vivo sites indicates flexibility in AbrB binding and recognition of three-dimensional DNA structures.
Mol Microbiol: 1996, 19(1);145-58
[PubMed:8821944] [WorldCat.org] [DOI] (P p)

M A Strauch
AbrB modulates expression and catabolite repression of a Bacillus subtilis ribose transport operon.
J Bacteriol: 1995, 177(23);6727-31
[PubMed:7592460] [WorldCat.org] [DOI] (P p)

M Perego, G B Spiegelman, J A Hoch
Structure of the gene for the transition state regulator, abrB: regulator synthesis is controlled by the spo0A sporulation gene in Bacillus subtilis.
Mol Microbiol: 1988, 2(6);689-99
[PubMed:3145384] [WorldCat.org] [DOI] (P p)

1. Banse et al. (2008) Parallel pathways of repression and antirepression governing the transition to stationary phase in Bacillus subtilis.Proc. Natl. Acad. Sci. USA 105: 15547-15552. PubMed
2. Perego et al. (1988) Structure of the gene for the transition state regulator, abrB: regulator synthesis is controlled by the spo0A sporulation gene in Bacillus subtilis. Mol. Microbiol. 2: 689-699. PubMed
3. Xu, K. and M.A. Strauch. (1996) In vitro selection of optimal AbrB-binding sites: comparison to known in vivo sites indicates flexibility in AbrB-binding and recognition of three-dimensional DNA structures. Molec. Microbiol. 19: 145-158 PubMed
4. Xu, K., D. Clark and M.A. Strauch. (1996) Analysis of abrB mutations, mutant proteins, and why abrB does not utilize a perfect consensus in the –35 region of its sigmaA promoter.J. Biol. Chem. 271:2621-2626 PubMed
5. Vaughn, J.L., Feher V., Naylor, S., Strauch, M.A. and J. Cavanagh. (2000) Novel DNA binding domain and genetic regulation model of Bacillus subtilis transition state regulator AbrB. Nature Structural Biology 7:1139-1146; PubMed, Corrigendum appears in Nature Stuctural & Molecular Biology (2005) 12:380
6. Xu, K. and M.A. Strauch. (2001) DNA-binding activity of amino-terminal domains of the Bacillus subtilis AbrB protein. J. Bacteriol. 183:4094-4098 PubMed
7. Phillips, Z. E.V. and M.A. Strauch. (2001) Role of Cys54 in AbrB multimerization and DNA-binding activity. FEMS Microbiol. Letters. 203:207-210 PubMed
8. Phillips, Z.E.V. and M.A. Strauch. (2002) Bacillus subtilis sporulation and stationary phase gene expression. Cellular and Molecular Life Sciences 59:392-402 PubMed
9. Shafikhani, S.H., Mandic-Mulec, I., Strauch, M.A., Smith, I. and T. Leighton. (2002) Postexponential regulation of sin operon expression in Bacillus subtilis. J. Bacteriol. 184:564-571 PubMed
10. Benson, L. M., Vaughn, J. L., Strauch, M. A., Bobay, B. G., Thompson, R., Naylor, S. and J. Cavanagh (2002). Macromolecular assembly of the transition state regulator AbrB in its unbound and complexed states probed by microelectrospray ionization mass spectrometry. Analytical Biochemistry 306:222-227 PubMed
11. Qian, Q., Lee, C.Y., Helmann, J. and M.A. Strauch. (2002) AbrB regulation of the sigmaW regulon of Bacillus subtilis. FEMS Microbiol. Letters 211:219-223. PubMed
12. Kim, H. J., S. I. Kim, M. Ratnayake-Lecamwasam, K. Tachikawa, A. L. Sonenshein, and M. Strauch. (2003) Complex regulation of the Bacillus subtilis aconitase gene. J. Bacteriol. 185:1672-1680. PubMed
13. Bobay, B.G., Benson, L., Naylor, S., Feeney, B., Clark, A.C., Goshe, M.B., Strauch, M.A., Thompson, R., and J.Cavanagh. (2004) Evaluation of the DNA binding tendencies of the transition state regulator AbrB. Biochemistry. 43:16106-16118. PubMed
14. Bobay et al.(2005) Revised structure of the AbrB N-terminal domain unifies a diverse superfamily of putative DNA-binding proteins. FEBS Lett. 579:5669-5674. PubMed
15. Yao, F and M.A. Strauch (2005) Independent and Interchangeable Multimerization Domains of the AbrB, Abh and SpoVT Global Regulatory Proteins. J. Bacteriol. 187:6354-6362 PubMed
16. Bobay, B.G., Mueller, G.A., Thompson, R.J., Venters, R.A., Murzin, A.G., Strauch, M.A. & J. Cavanagh (2006) NMR structure of AbhN and comparison with AbrBN: First Insights into the DNA-binding Promiscuity and Specificity of AbrB-like Transition-state Regulator Proteins. J. Biol. Chem. 281:21399-21409 PubMed
17. Jordan S. Rietkötter E. Strauch MA. Kalamorz F. Butcher BG. Helmann JD. Mascher T. (2007) LiaRS-dependent gene expression is embedded in transition state regulation in Bacillus subtilis. Microbiology. 153: 2530-2540. PubMed
18. Strauch MA. Bobay BG. Cavanagh J. Yao F. Wilson A. Le Breton Y. (2007) Abh and AbrB control of Bacillus subtilis antimicrobial gene expression. J. of Bacteriol. 189:7720-7732. PubMed
19. Hamze et al. (2009) Identification of genes required for different stages of dendritic swarming in Bacillus subtilis, with a novel role for phrC. Microbiology 155: 398-412. PubMed
20. Strauch MA. (1995) AbrB modulates expression and catabolite repression of a Bacillus subtilis ribose transport operon. J Bacteriol. Dec;177(23):6727-31. PubMed
21. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed