The transcription factor alsr binds and regulates the promoter of the alssd operon responsible for acetoin formation in bacillus subtilis

Journal of Bacteriology

Volumn 194, Issue 5, 2012, Pages 1100-1112

  Frädrich, Claudia ^a   March, Anika ^a   Fiege, Kerstin ^a   Hartmann, Anja ^a   Jahn, Dieter ^a   Härtig, Elisabeth ^a  

^a TECHNICAL UNIVERSITY OF BRAUNSCHWEIG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ACETOIN; PALINDROMIC DNA; PROTEIN S 100; RNA POLYMERASE; S100A PROTEIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR ALSR; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; BACILLUS SUBTILIS; BACTERIAL GENE; BINDING AFFINITY; BINDING SITE; COMPLEX FORMATION; CONTROLLED STUDY; IN VITRO STUDY; IN VIVO STUDY; MUTAGENESIS; NONHUMAN; OPERON; PH; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN DNA BINDING; SEQUENCE ANALYSIS; TRANSCRIPTION INITIATION SITE; TRANSCRIPTION REGULATION;

ACETOIN; BACILLUS SUBTILIS; BINDING SITES; DNA MUTATIONAL ANALYSIS; DNA, BACTERIAL; GENE EXPRESSION REGULATION, BACTERIAL; MODELS, BIOLOGICAL; MUTANT PROTEINS; MUTATION, MISSENSE; OPERON; PROMOTER REGIONS, GENETIC; PROTEIN BINDING; TRANSCRIPTION FACTORS; TRANSCRIPTION, GENETIC;

BACILLUS SUBTILIS;

EID: 84857870558     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.06425-11     Document Type: Article

References (38)

1. Ausubel FM, et al. 1995. Current protocols in molecular biology. John Wiley & Sons Inc., New York, NY.
2. Bundy BM, Collier LS, Hoover TR, Neidle EL. 2002. Synergistic transcriptional activation by one regulatory protein in response to two metabolites. Proc. Natl. Acad. Sci. U. S. A. 99:7693-7698.
3. Collier LS, Gaines GL III, Neidle EL. 1998. Regulation of benzoate degradation in Acinetobacter sp. strain ADP1 by BenM, a LysR-type transcriptional activator. J. Bacteriol. 180:2493-2501.
4. Craven SH, et al. 2009. Inducer responses of BenM, a LysR-type transcriptional regulator from Acinetobacter baylyi ADP1. Mol. Microbiol. 72:881-894.
5. Cruz-Ramos H, et al. 2000. Fermentative metabolism of Bacillus subtilis: physiology and regulation of gene expression. J. Bacteriol. 182:3072-3080.
6. Engler-Blum G, Meier M, Frank J, Muller GA. 1993. Reduction of background problems in nonradioactive Northern and Southern blot analyses enables higher sensitivity than 32P-based hybridizations. Anal. Biochem. 210:235-244.
7. Ezezika OC, Collier-Hyams LS, Dale HA, Burk AC, Neidle EL. 2006. CatM regulation of the benABCDE operon: functional divergence of two LysR-type paralogs in Acinetobacter baylyi ADP1. Appl. Environ. Microbiol. 72:1749-1758.
8. Ezezika OC, Haddad S, Clark TJ, Neidle EL, Momany C. 2007. Distinct effector-binding sites enable synergistic transcriptional activation by BenM, a LysR-type regulator. J. Mol. Biol. 367:616-629.
9. Ezezika OC, Haddad S, Neidle EL, Momany C. 2007. Oligomerization of BenM, a LysR-type transcriptional regulator: structural basis for the aggregation of proteins in this family. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63:361-368.
10. Glaser P, Danchin A, Kunst F, Zuber P, Nakano MM. 1995. Identification and isolation of a gene required for nitrate assimilation and anaerobic growth of Bacillus subtilis. J. Bacteriol. 177:1112-1115.
11. Grundy FJ, Waters DA, Takova TY, Henkin TM. 1993. Identification of genes involved in utilization of acetate and acetoin in Bacillus subtilis. Mol. Microbiol. 10:259-271.
12. Härtig E, et al. 2004. Bacillus subtilis ResD induces expression of the potential regulatory genes yclJK upon oxygen limitation. J. Bacteriol. 186: 6477-6484.
13. Harwood CR, Cutting SM. 1990. Molecular biological methods for Bacillus subtilis. Wiley & Sons, Chichester, United Kingdom.
14. Hoffmann T, Troup B, Szabo A, Hungerer C, Jahn D. 1995. The anaerobic life of Bacillus subtilis: cloning of the genes encoding the respiratory nitrate reductase system. FEMS Microbiol. Lett. 131:219-225.
15. Holtzclaw WD, Chapman LF. 1975. Degradative acetolactate synthase of Bacillus subtilis: purification and properties. J. Bacteriol. 121:917-922.
16. Hornbaek T, Jakobsen M, Dynesen J, Nielsen AK. 2004. Global transcription profiles and intracellular pH regulation measured in Bacillus licheniformis upon external pH upshifts. Arch. Microbiol. 182:467-474.
17. Hryniewicz MM, Kredich NM. 1994. Stoichiometry of binding of CysB to the cysJIH, cysK, and cysP promoter regions of Salmonella typhimurium. J. Bacteriol. 176:3673-3682.
18. Kamimura N, et al. 2010. Regulatory system of the protocatechuate 4,5-cleavage pathway genes essential for lignin downstream catabolism. J. Bacteriol. 192:3394-3405.
19. Kitko RD, et al. 2009. Cytoplasmic acidification and the benzoate transcriptome in Bacillus subtilis. PLoS One 4:e8255.
20. Maddocks SE, Oyston PC. 2008. Structure and function of the LysR-type transcriptional regulator (LTTR) family proteins. Microbiology 154: 3609-3623.
21. Martin-Verstraete I, Debarbouille M, Klier A, Rapoport G. 1992. Mutagenesis of the Bacillus subtilis "-12,-24" promoter of the levanase operon and evidence for the existence of an upstream activating sequence. J. Mol. Biol. 226:85-99.
22. Miller JH. 1992.A short course in bacterial genetics: a laboratory manual and handbook for Escherichia coli and related bacteria. Cold Spring Harbor Laboratory Press, Plainville, NY.
23. Nakano MM, Dailly YP, Zuber P, Clark DP. 1997. Characterization of anaerobic fermentative growth of Bacillus subtilis: identification of fermentation end products and genes required for growth. J. Bacteriol. 179: 6749-6755.
24. Nakano MM, Zuber P. 1998. Anaerobic growth of a "strict aerobe" (Bacillus subtilis). Annu. Rev. Microbiol. 52:165-190.
25. Nicholson WL. 2008. The Bacillus subtilis ydjL (bdhA) gene encodes acetoin reductase/2,3-butanediol dehydrogenase. Appl. Environ. Microbiol. 74:6832-6838.
26. Presecan-Siedel E, et al. 1999. Catabolite regulation of the pta gene as part of carbon flow pathways in Bacillus subtilis. J. Bacteriol. 181:6889-6897.
27. Qi Y, Hulett FM. 1998. PhoP-P and RNA polymerase sigmaA holoenzyme are sufficient for transcription of Pho regulon promoters in Bacillus subtilis: PhoP-P activator sites within the coding region stimulate transcription in vitro. Mol. Microbiol. 28:1187-1197.
28. Reents H, et al. 2006. Bacillus subtilis Fnr senses oxygen via a [4Fe-4S]2_ cluster coordinated by three cysteine residues without change in the oligomeric state. Mol. Microbiol. 60:1432-1445.
29. Reents H, Munch R, Dammeyer T, Jahn D, Härtig E. 2006. The Fnr regulon of Bacillus subtilis. J. Bacteriol. 188:1103-1112.
30. Renna MC, Najimudin N, Winik LR, Zahler SA. 1993. Regulation of the Bacillus subtilis alsS, alsD, and alsR genes involved in post-exponentialphase production of acetoin. J. Bacteriol. 175:3863-3875.
31. Ruangprasert A, Craven SH, Neidle EL, Momany C. 2010. Full-length structures of BenM and two variants reveal different oligomerization schemes for LysR-type transcriptional regulators. J. Mol. Biol. 404:568-586.
32. Sainsbury S, et al. 2009. The structure of CrgA from Neisseria meningitidis reveals a new octameric assembly state for LysR transcriptional regulators. Nucleic Acids Res. 37:4545-4558.
33. Schell MA. 1993. Molecular biology of the LysR family of transcriptional regulators. Annu. Rev. Microbiol. 47:597-626.
34. Stec E, et al. 2006. Structural basis of the sulphate starvation response in E. coli: crystal structure and mutational analysis of the cofactor-binding domain of the Cbl transcriptional regulator. J. Mol. Biol. 364:309-322.
35. Sun G, et al. 1996. Regulators of aerobic and anaerobic respiration in Bacillus subtilis. J. Bacteriol. 178:1374-1385.
36. Tsau JL, Guffanti AA, Montville TJ. 1992. Conversion of pyruvate to acetoin helps to maintain pH homeostasis in Lactobacillus plantarum. Appl. Environ. Microbiol. 58:891-894.
37. Wilks JC, et al. 2009. Acid and base stress and transcriptomic responses in Bacillus subtilis. Appl. Environ. Microbiol. 75:981-990.
38. Zhou X, et al. 2010. Crystal structure of ArgP from Mycobacterium tuberculosis confirms two distinct conformations of full-length LysR transcriptional regulators and reveals its function in DNA binding and transcriptional regulation. J. Mol. Biol. 396:1012-1024.