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 |
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
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Contents
The gene
Basic information
- Coordinates:
Phenotypes of a mutant
No swarming motility on B medium. PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
Genes/ operons controlled by AbrB
- 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):
- 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]
Additional information
Expression and regulation
- Operon: abrB PubMed
- Regulation: expressed at the onset of stationary phase 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
Your additional remarks
References
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Strauch MA. (1995) AbrB modulates expression and catabolite repression of a Bacillus subtilis ribose transport operon. J Bacteriol. Dec;177(23):6727-31. PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed