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| * '''Description:''' transition state regulator<br/><br/>
| | {{#bank: AbrB}} |
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| {| align="right" border="1" cellpadding="2"
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| |style="background:#ABCDEF;" align="center"|'''Gene name'''
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| |''abrB''
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| |style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''cpsX ''
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| |style="background:#ABCDEF;" align="center"| '''Essential''' ||
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| |style="background:#ABCDEF;" align="center"| '''Product''' || transcriptional regulator
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| |style="background:#ABCDEF;" align="center"|'''Function''' || regulation of transition state genes
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| |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 10 kDa, 6.57
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| |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 288 bp, 96 aa
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| |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' ||
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| |style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/abrB_nucleotide.txt Gene sequence (+200bp) ]'''
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| |style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/abrB_protein.txt Protein sequence]'''
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| |colspan="2" | '''Genetic context''' <br/> [[Image:abrB_context.gif]]
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| |}
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| __TOC__
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| <br/><br/>
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| =The gene=
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| === Basic information ===
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| * '''Coordinates:'''
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| ===Phenotypes of a mutant ===
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| === Database entries ===
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| * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/abrB.html]
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| * '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG10100]
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| === Additional information===
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| =The protein=
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| === Basic information/ Evolution ===
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| * '''Catalyzed reaction/ biological activity:'''
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| * '''Protein family:'''
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| * '''Paralogous protein(s):''' [[Abh]], [[SpoVT]] (only N-terminal domain)
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| === Extended information on the protein ===
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| * '''Kinetic information:'''
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| * '''Domains:'''
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| * '''Modification:'''
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| * '''Cofactor(s):'''
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| * '''Effectors of protein activity:''' interaction with [[AbbA]] results in inactivation of AbrB [http://www.ncbi.nlm.nih.gov/sites/entrez/18840696 PubMed]
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| * '''Interactions:''' [[AbrB]]-[[AbbA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/18840696 PubMed]
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| * '''Localization:'''
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| === Database entries ===
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| * '''Structure:''' 1Z0R (N-terminal DNA recognition domain) [http://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?Dopt=s&uid=32611 NCBI] [http://www.ncbi.nlm.nih.gov/sites/entrez/16223496 PubMed]
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| * '''Swiss prot entry:'''
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| * '''KEGG entry:'''
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| === Additional information===
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| negative regulation of ''[[abrB]], [[aprE]], [[ftsAZ]], [[kinC]], [[motA]], [[nprE]], [[pbpE]], [[rbs]], [[spo0H]], [[spoVG]], [[spo0E]], [[tycA]], [[sbo]]-[[alb]], [[yqxM]]-[[sipW]]-[[tasA]]'';
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| positive regulation of ''[[comK]], [[hpr]]''
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| =Expression and regulation=
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| * '''Operon:'''
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| * '''Sigma factor:'''
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| * '''Regulation:''' expressed at the onset of staionary phase
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| * '''Regulatory mechanism:''' repressed by [[Spo0A]]-P
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| * '''Additional information:'''
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| =Biological materials =
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| * '''Mutant:''' TT731 (aphA3)
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| * '''Expression vector:'''
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| * '''lacZ fusion:'''
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| * '''GFP fusion:'''
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| * '''two-hybrid system:'''
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| * '''Antibody:'''
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| =Labs working on this gene/protein=
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| [[Richard Losick]], Harvard Univ., Cambridge, USA [http://www.mcb.harvard.edu/Losick/ homepage]
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| [[Mark Strauch]], Baltimore, USA [http://lifesciences.umaryland.edu/Pages/faculty_profile.aspx?ID=212 homepage]
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| =Your additional remarks=
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| =References=
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| # 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/18840696 PubMed]
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| # 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 [http://www.ncbi.nlm.nih.gov/sites/entrez/8821944 PubMed]
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| # 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 [http://www.ncbi.nlm.nih.gov/sites/entrez/8576231 PubMed]
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| # 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; [http://www.ncbi.nlm.nih.gov/sites/entrez/11101897 PubMed], Corrigendum appears in Nature Stuctural & Molecular Biology (2005) 12:380
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| # 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 [http://www.ncbi.nlm.nih.gov/sites/entrez/11395475 PubMed]
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| # 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 [http://www.ncbi.nlm.nih.gov/sites/entrez/11583849 PubMed]
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| # 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 [http://www.ncbi.nlm.nih.gov/sites/entrez/11964117 PubMed]
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| # 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 [http://www.ncbi.nlm.nih.gov/sites/entrez/11751836 PubMed]
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| # 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 [http://www.ncbi.nlm.nih.gov/sites/entrez/12123659 PubMed]
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| # 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/12076816 PubMed]
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| # 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/12591885 PubMed]
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| # 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/15610005 PubMed]
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| # 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/16223496 PubMed]
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| # 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 [http://www.ncbi.nlm.nih.gov/sites/entrez/16159768 PubMed]
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| # 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 [http://www.ncbi.nlm.nih.gov/sites/entrez/16702211 PubMed]
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| # 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/17660417 PubMed]
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| # 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/17720793 PubMed]
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