The type III pantothenate kinase encoded by coaX is essential for growth of Bacillus anthracis

Journal of Bacteriology

Volumn 190, Issue 18, 2008, Pages 6271-6275

  Paige, Carleitta ^a   Reid, Sean D ^a   Hanna, Philip C ^b   Claiborne, Al ^a  

^a WAKE FOREST SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; COENZYME A; PANTOTHENATE KINASE; PANTOTHENATE KINASE TYPE III; UNCLASSIFIED DRUG;

ARTICLE; BACILLUS ANTHRACIS; BACTERIAL GENE; BACTERIAL GENETICS; BACTERIAL GROWTH; CATALYSIS; COENZYME AX GENE; DRUG TARGETING; ENZYME SYNTHESIS; GENE CLUSTER; MUTANT; NONHUMAN; PRIORITY JOURNAL;

BACILLUS ANTHRACIS; BACTERIAL PROTEINS; BASE SEQUENCE; GENE EXPRESSION REGULATION, BACTERIAL; MOLECULAR SEQUENCE DATA; MUTATION; OPERON; PHOSPHOTRANSFERASES (ALCOHOL GROUP ACCEPTOR); PROMOTER REGIONS (GENETICS);

BACILLUS ANTHRACIS;

EID: 51549083825     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00860-08     Document Type: Article

References (37)

1. Altschul, S. F., W. Gish, W. Miller, E. W. Myers, and D. J. Lipman. 1990. Basic local alignment search tool. J. Mol. Biol. 215:403-410.
2. Antelmann, H., R. C. Williams, M. Miethke, A. Wipat, D. Albrecht, C. R. Harwood, and M. Hecker. 2005. The extracellular and cytoplasmic proteomes of the non-virulent Bacillus anthracis strain UM23C1-2. Proteomics 5:3684-3695.
3. Bergman, N. H., E. C. Anderson, E. E. Swenson, B. K. Janes, N. Fisher, M. M. Niemeyer, A. D. Miyoshi, and P. C. Hanna. 2007. Transcriptional profiling of Bacillus anthracis during infection of host macrophages. Infect. Immun. 75:3434-3444.
4. Bergman, N. H., E. C. Anderson, E. E. Swenson, M. M. Niemeyer, A. D. Miyoshi, and P. C. Hanna. 2006. Transcriptional profiling of the Bacillus anthracis life cycle in vitro and an implied model for regulation of spore formation. J. Bacteriol. 188:6092-6100.
5. Bergman, N. H., K. D. Passalacqua, P. C. Hanna, and Z. S. Qin. 2007. Operon prediction for sequenced bacterial genomes without experimental information. Appl. Environ. Microbiol. 73:846-854.
6. Brand, L. A., and E. Strauss. 2005. Characterization of a new pantothenate kinase isoform from Helicobacter pylori. J. Biol. Chem. 280:20185-20188.
7. Chattopadhyay, A., M. Meier, S. Ivaninskii, P. Burkhard, F. Speroni, B. Campanini, S. Bettati, A. Mozzarelli, W. M. Rabeh, L. Li, and P. F. Cook. 2007. Structure, mechanism, and conformational dynamics of O-acetylserine sulfhydrylase from Salmonella typhimurium: comparison of A and B isozymes. Biochemistry 46:8315-8330.
8. Fahey, R. C. 2001. Novel thiols of prokaryotes. Annu. Rev. Microbiol. 55: 333-356.
9. Fisher, N., and P. Hanna. 2005. Characterization of Bacillus anthracis germinant receptors in vitro. J. Bacteriol. 187:8055-8062.
10. Gerdes, S. Y., M. D. Scholle, M. D'Souza, A. Bernal, M. V. Baev, M. Farrell, O. V. Kurnasov, M. D. Daugherty, F. Mseeh, B. M. Polanuyer, J. W. Campbell, S. Anantha, K. Y. Shatalin, S. A. Chowdhury, M. Y. Fonstein, and A. L. Osterman. 2002. From genetic footprinting to antimicrobial drug targets: examples in cofactor biosynthetic pathways. J. Bacteriol. 184:4555-4572.
11. Harwood, C. R., and R. Cranenburgh. 2008. Bacillus protein secretion: an unfolding story. Trends Microbiol. 16:73-79.
12. Helmann, J. D. 1995. Compilation and analysis of Bacillus subtilis sigma A-dependent promoter sequences: evidence for extended contact between RNA polymerase and upstream promoter DNA. Nucleic Acids Res. 23: 2351-2360.
13. Hochgräfe, F., J. Mostertz, D.-C. Pother, D. Becher, J. D. Helmann, and M. Hecker. 2007. S-Cysteinylation is a general mechanism for thiol protection of Bacillus subtilis proteins after oxidative stress. J. Biol. Chem. 282:25981-25985.
14. Hong, B. S., G. Senisterra, W. M. Rabeh, M. Vedadi, R. Leonardi, Y.-M. Zhang, C. O. Rock, S. Jackowski, and H.-W. Park. 2007. Crystal structures of human pantothenate kinases: insights into allosteric regulation and mutations linked to a neurodegeneration disorder. J. Biol. Chem. 282:27984-27993.
15. Hong, B. S., M. K. Yun, Y. M. Zhang, S. Chohnan, C. O. Rock, S. W. White, S. Jackowski, H. W. Park, and R. Leonardi. 2006. Prokaryotic type II and type III pantothenate kinases: the same monomer fold creates dimers with distinct catalytic properties. Structure 14:1251-1261.
16. Hullo, M.-F., S. Auger, O. Soutourina, O. Barzu, M. Yvon, A. Danchin, and I. Martin-Verstraete. 2007. Conversion of methionine to cysteine in Bacillus subtilis and its regulation. J. Bacteriol. 189:187-197.
17. Janes, B. K., and S. Stibitz. 2006. Routine markerless gene replacement in Bacillus anthracis. Infect. Immun. 74:1949-1953.
18. Leichert, L. I., C. Scharf, and M. Hecker. 2003. Global characterization of disulfide stress in Bacillus subtilis. J. Bacteriol. 185:1967-1975.
19. Leonardi, R., S. Chohnan, Y. M. Zhang, K. G. Virga, R. E. Lee, C. O. Rock, and S. Jackowski. 2005. A pantothenate kinase from Staphylococcus aureus refractory to feedback regulation by coenzyme A. J. Biol. Chem. 280:3314-3322.
20. Leonardi, R., Y. M. Zhang, C. O. Rock, and S. Jackowski. 2005. Coenzyme A: back in action. Prog. Lipid Res. 44:125-153.
21. Liu, H., N. H. Bergman, B. Thomason, S. Shallom, A. Hazen, J. Crossno, D. A. Rasko, J. Ravel, T. D. Read, S. N. Peterson, J. Yates III, and P. C. Hanna. 2004. Formation and composition of the Bacillus anthracis endospore. J. Bacteriol. 186:164-178.
22. Mountain, A. 1989. Gene expression systems for Bacillus subtilis, p. 73-114. In C. R. Harwood (ed.), Bacillus, vol. 2. Plenum Press, New York, NY.
23. Newton, G. L., K. Arnold, M. S. Price, C. Sherrill, S. B. delCardayre, Y. Aharonowitz, G. Cohen, J. Davies, R. C. Fahey, and C. Davis. 1996. Distribution of thiols in microorganisms: mycothiol is a major thiol in most actinomycetes. J. Bacteriol. 178:1990-1995.
24. Newton, G. L., and R. C. Fahey. 1990. Glutathione in prokaryotes, p. 69-77. In J. Vina (ed.), Glutathione: metabolism and physiological functions. CRC Press, Boca Raton, FL.
25. Nicely, N. I., D. Parsonage, C. Paige, G. L. Newton, R. C. Fahey, R. Leonardi, S. Jackowski, T. C. Mallett, and A. Claiborne. 2007. Structure of the type III pantothenate kinase from Bacillus anthracis at 2.0 Å resolution: implications for coenzyme A-dependent redox biology. Biochemistry 46:3234-3245.
26. Overbeek, R., T. Begley, R. M. Butler, J. V. Choudhuri, H. Y. Chuang, M. Cohoon, V. de Crecy-Lagard, N. Diaz, T. Disz, R. Edwards, M. Fonstein, E. D. Frank, S. Gerdes, E. M. Glass, A. Goesmann, A. Hanson, D. Iwata-Reuyl, R. Jensen, N. Jamshidi, L. Krause, M. Kubal, N. Larsen, B. Linke, A. C. McHardy, F. Meyer, H. Neuweger, G. Olsen, R. Olson, A. Osterman, V. Portnoy, G. D. Pusch, D. A. Rodionov, C. Ruckert, J. Steiner, R. Stevens, I. Thiele, O. Vassieva, Y. Ye, O. Zagnitko, and V. Vonstein. 2005. The subsystems approach to genome annotation and its use in the project to annotate 1000 genomes. Nucleic Acids Res. 33:5691-5702.
27. Prágai, Z., and C. R. Harwood. 2000. YsxC, a putative GTP-binding protein essential for growth of Bacillus subtilis 168. I. Bacteriol. 182:6819-6823.
28. Sadler, J. R., H. Sasmor, and J. L. Betz. 1983. A perfectly symmetric lac operator binds the lac repressor very tightly. Proc. Natl. Acad. Sci. USA 80:6785-6789.
29. Schnell, R., W. Oehlmann, M. Singh, and G. Schneider. 2007. Structural insights into catalysis and inhibition of O-acetylserine sulfhydrylase from Mycobacterium tuberculosis. Crystal structures of the enzyme α-aminoacrylate intermediate and an enzyme-inhibitor complex. J. Biol. Chem. 282: 23473-23481.
30. Setlow, B., and P. Setlow. 1977. Levels of acetyl coenzyme A, reduced and oxidized coenzyme A, and coenzyme A in disulfide linkage to protein in dormant and germinated spores and growing and sporulating cells of Bacillus megaterium. J. Bacteriol. 132:444-452.
31. Spry, C., K. Kirk, and K. J. Saliba. 2008. Coenzyme A biosynthesis: an antimicrobial drug target. FEMS Microbiol. Rev. 32:56-106.
32. Swerdlow, R. D., and P. Setlow. 1983. Purification and characterization of a Bacillus megaterium disulfide reductase specific for disulfides containing pantcthine 4′,4″-diphosphate. I. Bacteriol. 153:475-484.
33. Vrjayalakshmi, J., M. K. Mukhergee, J. Graumann, U. Jakob, and M. A. Saper. 2001. The 2.2 Å crystal structure of Hsp33: a heat shock protein with redox-regulated chaperone activity. Structure 9:367-375.
34. Wallen, J. R., C. Paige, T. C. Mallett, P. A. Karplus, and A. Claiborne. 2008. Pyridine nucleotide complexes with Bacillus anthracis coenzyme A-disulfide reductase: a structural analysis of dual NAD(P)H specificity. Biochemistry 47:5182-5193.
35. Yang, K., Y. Eyobo, L. A. Brand, D. Martynowski, D. Tomchick, E. Strauss, and H. Zhang. 2006. Crystal structure of a type III pantothenate kinase: insight into the mechanism of an essential coenzyme A biosynthetic enzyme universally distributed in bacteria. I. Bacteriol. 188:5532-5540.
36. Yang, K., E. Strauss, C. Huerta, and H. Zhang. 2008. Structural basis for substrate binding and the catalytic mechanism of type III pantothenate kinase. Biochemistry 47:1369-1380.
37. Yocum, R. R., and T. A. Patterson. December 2004. Microorganisms and assays for the identification of antibiotics. U.S. patent 6,830,898.