Role of the hprT-ftsH locus in Staphylococcus aureus

Microbiology

Volumn 150, Issue 2, 2004, Pages 373-381

  Lithgow, James K ^a   Ingham, Eileen ^b   Foster, Simon J ^a  

^a UNIVERSITY OF SHEFFIELD   (United Kingdom)

^b UNIVERSITY OF LEEDS   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ACID; ADENOSINE TRIPHOSPHATE; AMINO ACID; BETA GALACTOSIDASE; HYPOXANTHINE PHOSPHORIBOSYLTRANSFERASE; PARAQUAT; PHOSPHATE; POTASSIUM DERIVATIVE; PROTEINASE; SODIUM CHLORIDE; ZINC ION;

ARTICLE; ATTENUATION; BACTERIAL CHROMOSOME; BACTERIAL GROWTH; BACTERIAL SURVIVAL; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; DISEASE MODEL; GENE EXPRESSION; GENE FUNCTION; GENE IDENTIFICATION; GENE LOCUS; GENE MUTATION; GENETIC CODE; GROWTH INHIBITION; MEMBRANE BINDING; MUTAGENESIS; NONHUMAN; PATHOGENICITY; PLEIOTROPY; PRIORITY JOURNAL; PROTEIN SECRETION; SENSITIVITY ANALYSIS; SEQUENCE HOMOLOGY; SKIN INFECTION; STAPHYLOCOCCUS AUREUS; STARVATION; STRESS; TRANSPOSON;

BACTERIA (MICROORGANISMS); MURINAE; POSIBACTERIA; PROKARYOTA; STAPHYLOCOCCUS; STAPHYLOCOCCUS AUREUS; TRANSPOSONS;

EID: 1242296225     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.26674-0     Document Type: Article

References (41)

1. Akiyama, Y., Ogura, T. & Ito, K. (1994). Involvement of FtsH in protein assembly into and through the membrane. I. Mutations that reduce retention efficiency of a cytoplasmic reporter. J Biol Chem 269, 5218-5224.
2. 0 sector is a substrate of the FtsH protease in Escherichia coli. FEBS Lett 399, 26-28.
3. Akiyama, Y., Kihara, A., Tokuda, H. & Ito, K. (1996b). FtsH (HflB) is an ATP-dependent protease selectively acting on SecY and some other membrane proteins. J Biol Chem 271, 31196-31201.
4. Cassels, R., Oliva, B. & Knowles, D. (1995). Occurrence of the regulatory nucleotides ppGpp and pppGpp following induction of the stringent response in staphylococci. J Bacteriol 177, 5161-5165.
5. B controls the environmental stress response but not starvation survival or pathogenicity in a mouse abscess model. J Bacteriol 180, 6082-6089.
6. Clements, M. & Foster, S. (1999). Stress resistance in Staphylococcus aureus. Trends Microbiol 7, 458-462.
7. Clements, M. O., Watson, S. P. & Foster, S. J. (1999a). Characterization of the major superoxide dismutase of Staphylococcus aureus and its role in starvation survival, stress resistance, and pathogenicity. J Bacteriol 181, 3898-3903.
8. Clements, M. O., Watson, S., Poole, R. K. & Foster, S. J. (1999b). CtaA of Staphylococcus aureus is required for starvation survival, recovery, and cytochrome biosynthesis. J Bacteriol 181, 501-507.
9. Deuerling, E., Mogk, A., Richter, C., Purucker, M. & Schumann, W. (1997). The ftsH gene of Bacillus subtilis is involved in major cellular processes such as sporulation, stress adaptation and secretion. Mol Microbiol 23, 921-933.
10. Fischer, B., Rummel, G., Aldridge, P. & Jenal, U. (2002). The FtsH protease is involved in development, stress response and heat shock control in Caulobacter crescentus. Mol Microbiol 44, 461-478.
11. Forsyth, R. A., Haselbeck, R. J., Ohlsen, K. L. & 20 other authors (2002). A genome-wide strategy for the identification of essential genes in Staphylococcus aureus. Mol Microbiol 43, 1387-1400.
12. Ge, Z. & Taylor, D. E. (1996). Sequencing, expression, and genetic characterization of the Helicobacter pylori ftsH gene encoding a protein homologous to members of a novel putative ATPase family. J Bacteriol 178, 6151-6157.
13. Gentry, D., Li, T., Rosenberg, M. & McDevitt, D. (2000). The rel gene is essential for in vitro growth of Staphylococcus aureus. J Bacteriol 182, 4995-4997.
14. Guérout-Fleury, A. M., Shazand, K., Frandsen, N. & Stragier, P. (1995). Antibiotic-resistance cassettes for Bacillus subtilis. Gene 167, 335-336.
15. 32, the heat shock regulator in Escherichia coli, is governed by HflB. Proc Natl Acad Sci U S A 92, 3516-3520.
16. B modulates virulence determinant expression and stress resistance: characterization of a functional rsbU strain derived from Staphylococcus aureus 8325-4. J Bacteriol 184, 5457-5467.
17. Horsburgh, M. J., Wharton, S. J., Cox, A. G., Ingham, E., Peacock, S. & Foster, S. J. (2002b). MntR modulates expression of the PerR regulon and superoxide resistance in Staphylococcus aureus through control of manganese uptake. Mol Microbiol 44, 1269-1286.
18. Kemp, E. H., Sammons, R. L., Moir, A., Sun, D. & Setlow, P. (1991). Analysis of transcriptional control of the gerD spore germination gene of Bacillus subtilis 168. J Bacteriol 173, 4646-4652.
19. Kihara, A., Akiyama, Y. & Ito, K. (1995). FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit. Proc Natl Acad Sci U S A 92, 4532-4536.
20. Kobayashi, K., Ehrlich, S. D., Albertini, A. & 96 other authors (2003). Essential Bacillus subtilis genes. Proc Natl Acad Sci U S A 100, 4678-4683.
21. Konarska-Kozlowska, M. & Iyer, V. N. (1981). Physical and genetic organization of the IncN-group plasmid pCU1. Gene 14, 195-204.
22. Kuroda, M., Ohta, T., Uchiyama, I. & 34 other authors (2001). Whole genome sequencing of methicillin-resistant Staphylococcus aureus. Lancet 357, 1225-1240.
23. Langer, T. (2000). AAA proteases: cellular machines for degrading membrane proteins. Trends Biochem Sci 25, 247-251.
24. Lowy, F. D. (1998). Staphylococcus aureus infections. N Engl J Med 339, 520-532.
25. Lysenko, E., Ogura, T. & Cutting, S. M. (1997). Characterization of the ftsH gene of Bacillus subtilis. Microbiology 143, 971-978.
26. Nilsson, D., Lauridsen, A. A., Tomoyasu, T. & Ogura, T. (1994). A Lactococcus lactis gene encodes a membrane protein with putative ATPase activity that is homologous to the essential Escherichia coli ftsH gene product. Microbiology 140, 2601-2610.
27. Novick, R. P. (1991). Genetic systems in staphylococci. Methods Enzymol 204, 587-636.
28. Nygaard, P. (1993). Purine and pyrimidine salvage pathways. In Bacillus subtilis and Other Gram-Positive Bacteria, pp. 359-378. Edited by A. L. Sonenshein, J. A. Hoch & R. Losick. Washington, DC: American Society for Microbiology.
29. Ogura, T. & Wilkinson, A. J. (2001). AAA+ superfamily ATPases: common structure-diverse function. Genes Cells 6, 575-597.
30. Ogura, T., Tomoyasu, T., Yuki, T., Morimura, S., Begg, K. J., Donachie, W. D., Mori, H., Niki, H. & Hiraga, S. (1991). Structure and function of the ftsH gene in Escherichia coli. Res Microbiol 142, 279-282.
31. Sambrook, J., Fritsch, E. F. & Maniatis, T. (1989). Molecular Cloning: a Laboratory Manual, 2nd edn. Cold Spring Harbor, NY: Cold Spring Laboratory.
32. Schenk, S. & Laddaga, R. A. (1992). Improved method for electroporation of Staphylococcus aureus. FEMS Microbiol Lett 73, 133-138.
33. Schumann, W. (1999). FtsH - a single-chain charonin? FEMS Microbiol Rev 23, 1-11.
34. Shirai, Y., Akiyama, Y. & Ito, K. (1996). Suppression of ftsH mutant phenotypes by overproduction of molecular chaperones. J Bacteriol 178, 1141-1145.
35. Taylor, D. (1999). Bacterial tellurite resistance. Trends Microbiol 7, 111-115.
36. Taylor, C. M., Beresford, M., Epton, H. A., Sigee, D. C., Shama, G., Andrew, P. W. & Roberts, I. S. (2002). Listeria monocytogenes relA and hpt mutants are impaired in surface-attached growth and virulence. J Bacteriol 184, 621-628.
37. Tomoyasu, T., Yuki, T., Morimura, S., Mori, H., Yamanaka, K., Niki, H., Hiraga, S. & Ogura, T. (1993). The Escherichia coli FtsH protein is a prokaryotic member of a protein family of putative ATPases involved in membrane functions, cell cycle control, and gene expression. J Bacteriol 175, 1344-1351.
38. 32. EMBO J 14, 2551-2560.
39. Watson, S. P., Antonio, M. & Foster, S. J. (1998a). Isolation and characterization of Staphylococcus aureus starvation-induced, stationary-phase mutants defective in survival or recovery. Microbiology 144, 3159-3169.
40. Watson, S. P., Clements, M. O. & Foster, S. J. (1998b). Characterization of the starvation-survival response of Staphylococcus aureus. J Bacteriol 180, 1750-1758.
41. W-controlled pbpE gene, resulting in filamentous growth of Bacillus subtilis. J Bacteriol 185, 973-982.