The dimeric repressor SoxR binds cooperatively to the promoter(s) regulating expression of the sulfur oxidation (sox) operon of Pseudaminobacter salicylatoxidans KCT001

Microbiology

Volumn 153, Issue 1, 2007, Pages 80-91

  Mandal, Sukhendu ^a   Chatterjee, Sujoy ^a   Dam, Bomba ^a   Roy, Pradosh ^a   Das Gupta, Sujoy K ^a  

^a BOSE INSTITUTE   (India)

Author keywords

[No Author keywords available]

Indexed keywords

DNA BINDING PROTEIN; PERIPLASMIC PROTEIN; SOXR PROTEIN; SULFUR; THIOSULFATE; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL STRAIN; BINDING AFFINITY; CONTROLLED STUDY; DNA BINDING; ESCHERICHIA COLI; GENE EXPRESSION REGULATION; GENE FUNCTION; GENE INSERTION; GENE LOCATION; GENE REPRESSION; GENE STRUCTURE; GENETIC CODE; MICROBIAL ACTIVITY; MUTAGENESIS; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROMOTER REGION; PSEUDAMINOBACTER SALICYLATOXIDANS; SULFUR OXIDIZING BACTERIUM;

ALPHAPROTEOBACTERIA; BACTERIAL PROTEINS; BASE SEQUENCE; BINDING SITES; DIMERIZATION; DNA, BACTERIAL; DNA-BINDING PROTEINS; MOLECULAR SEQUENCE DATA; OPERON; OXIDATION-REDUCTION; PROMOTER REGIONS (GENETICS); REPRESSOR PROTEINS; SULFUR; TRANS-ACTIVATORS; TRANSCRIPTION FACTORS;

ESCHERICHIA; PSEUDAMINOBACTER SALICYLATOXIDANS;

EID: 33846319411     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.29197-0     Document Type: Article

References (24)

1. Appie-Ayme, C. & Barks, B. C. (2002). SoxV, an orthologue of the CcdA disulfide transporter, is involved in thiosulfate oxidation in Rhodovulum sulfidophilum and reduces the periplasmic thioredoxin SoxW. Biochem Biophys Res Commun 296, 737-741.
2. Appia-Ayme, C, Little, P. J., Matsumoto, Y., Leech, A. P. & Barks, B. C. (2001). Cytochrome complex essential for photosynthetic oxidation of both thiosulfate and sulfide in Rhodovulum sulfidophilum. J Bacteriol 183, 6107-6118.
3. Bagchi, A., Roy, D. & Roy, P. (2005). Homology modeling of a transcriptional regulator SoxR of the lithotrophic sulfur oxidation (Sox) operon in α-Proteobacteria. J Biomol Struct Dyn 22, 571-578.
4. Bardischewsky, F. & Friedrich, C. G. (2001). The shxVW locus is essential for oxidation of inorganic sulfur and molecular hydrogen by Paracoccus pantotrophus GB17: a novel function for lithotrophy. FEMS Microbiol Lett 202, 215-220.
5. Bullock W. O, Fernandez, J. M. & Short, J. M. (1987). XL1-Blue: a high efficiency plasmid transforming recA Escherichia coli strains with beta-gatactosidase selection. BioTechniques 5, 376-378.
6. Deb, C, Stackebrandt, E., Padella, S., Saha, A. & Roy, P. (2004). Phylogenetically diverse new sulfur chemolithotrophs of α-Proteobacteria isolated from Indian soils. Curr Microbiol 48, 452-458.
7. Friedrich, C. G. (1998). Physiology and genetics of sulfur-oxidizing bacteria. Adv Microb Physiol 39, 235-289.
8. Friedrich, C. G, Quentmeier, A., Bardischewsky, F., Rother, D., Kraft, P., Kostka, S. & Prinz, H. (2000). Novel genes coding for lithotrophic sulfur oxidation of Paracoccus pantotrophus GB17. J Bacteriol 182, 4677-4687.
9. Friedrich, C. G., Rother, D., Bardischewsky, F., Quentmeler, A. & Fischer, J. (2001). Oxidation of reduced inorganic sulfur compounds by bacteria: emergence of a common mechanism? Appl Environ Microbiol 67, 2873-2882.
10. Jain, S., Kaushal, D., Dasgupta, S. K. & Tyagi, A. K. (1997). Construction of shuttle vectors for genetic manipulation and molecular analysis of mycobacteria. Gene 190, 37-44.
11. Kelly, D. P. (1989). Physiology and biochemistry of unicellular sulfur bacteria. In Autotrophic Bacteria, pp. 193-217. Edited by H. G. Schlegel & B. Bowien. Madison, WI: Springer-Verlag, Berlin Science Tech Publishers.
12. Lahiri, C. Mandal, S, Ghosh, W, Dam, B. & Roy, P. (2006). A novel gene cluster soxSRT is essential for the chemolithotrophic oxidation of thiosulfate and tetrathionate by Pseudaminobacter salicylatoxidans KCT001. Curr Microbiol 54, 267-273.
13. Meulenberg, R, Pronk J. T., Hazeu, W., Bos, P. & Kuenen, J. G. (1992). Oxidation of reduced sulfur compounds by intact cells of Thiobacillus acidophilus. Arch Microbiol 157, 161-168.
14. Miller, J. H. (1972). Experiments in Molecular Genetics, pp. 352-355, 403-404. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory.
15. Miller, V. L & Mekalanos, J. J. (1988). A novel suicide vector and its use in construction of insertion mutations: osmoregulation of outer membrane proteins and virulence determinants in Vibrio cholerae requires toxR. J Bacteriol 170, 2575-2583.
16. Mukhopadhyaya, P. N., Deb, C., Lahirl, C. & Roy, P. (2000). A soxA gene, encoding a diheme cytochrome c, and a sox locus, essential for sulfur oxidation in a new sulfur lithotrophic bacterium. J Bacteriol 182, 4278-4287.
17. Randall, J. C. & Coen, D. M. (2004). The herpes simplex virus processivity factor, UL42, binds DNA as a monomer. J Mol Biol 335, 409-413.
18. Rother, D, Henrich, H. J., Quentmeier, A., Bardischewsky, F. & Friedrich, C. G. (2001). Novel genes of the sox gene duster, mutagenesis of the flavoprotein SoxF, and evidence for a general sulfur-oxidizing system in Paracoccus pantotrophus GB17. J Bacteriol 183, 4499-4508.
19. Rother, D., Orawski, G., Bardischewsky, F. & Friedrich, C. G. (2005). SoxRS-mediated regulation of chemolithotrophic sulfur oxidation in Paracoccus pantotrophus. Microbiology 151, 1707-1716.
20. Sambrook J. & Russell, D. W. (2001). Molecular Cloning. a Laboratory Manual 2nd edn. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory.
21. Shore, D, Langowski, J. & Baldwin, R. (1981). DNA flexibility studied by covalent closure of short fragments into circles. Proc Natl Acad Sci U S A 78, 4833-4837.
22. Skorupski, K. & Taylor, R. K. (1996). Positive selection vectors for allelic exchange. Gene 169, 47-52.
23. Towbin, H., Staehelin, T. & Gordon, J. (1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A 76, 4350-4354.
24. Vishniac, W. & Santer, M. (1957). The thiobacilli. Bacteriol Rev 21, 195-213.