• [1]
    Andrews, S.C., Robinson, A.K., Rodriguez-Quinones, F. (2003) Bacterial iron homeostasis. FEMS Microbiol. Rev. 27, 215237.
  • [2]
    Smith, J.L. (2004) The physiological role of ferritin-like compounds in bacteria. Crit. Rev. Microbiol. 30, 173185.
  • [3]
    Glaser, P., Frangeul, L., Buchrieser, C., Rusniok, C., Amend, A., Baquero, F., Berche, P., Bloecker, H., Brandt, P., Chakraborty, T., Charbit, A., Chetouani, F., Couve, E., de Daruvar, A., Dehoux, P., Domann, E., Dominguez-Bernal, G., Duchaud, E., Durant, L., Dussurget, O., Entian, K.D., Fsihi, H., Garcia-del Portillo, F., Garrido, P., Gautier, L., Goebel, W., Gomez-Lopez, N., Hain, T., Hauf, J., Jackson, D., Jones, L.M., Kaerst, U., Kreft, J., Kuhn, M., Kunst, F., Kurapkat, G., Madueno, E., Maitournam, A., Vicente, J.M., Ng, E., Nedjari, H., Nordsiek, G., Novella, S., de Pablos, B., Perez-Diaz, J.C., Purcell, R., Remmel, B., Rose, M., Schlueter, T., Simoes, N., Tierrez, A., Vazquez-Boland, J.A., Voss, H., Wehland, J., Cossart, P. (2001) Comparative genomics of Listeria species. Science 294, 849852.
  • [4]
    Phan-Thanh, L., Gormon, T. (1995) Analysis of heat and cold shock proteins in Listeria by two-dimensional electrophoresis. Electrophoresis 16, 444450.
  • [5]
    Phan-Thanh, L., Gormon, T. (1997) Stress proteins in Listeria monocytogenes. Electrophoresis 18, 14641471.
  • [6]
    Hebraud, M., Guzzo, J. (2000) The main cold shock protein of Listeria monocytogenes belongs to the family of ferritin-like proteins. FEMS Microbiol. Lett. 190, 2934.
  • [7]
    Bozzi, M., Mignogna, G., Stefanini, S., Barra, D., Longhi, C., Valenti, P., Chiancone, E. (1997) A novel non-heme iron-binding ferritin related to the DNA-binding proteins of the Dps family in Listeria innocua. J. Biol. Chem. 272, 32593265.
  • [8]
    Polidoro, M., de Biase, D., Montagnini, B., Guarrera, L., Cavallo, S., Valenti, P., Stefanini, S., Chiancone, E. (2002) The expression of the dodecameric ferritin in Listeria spp. is induced by iron limitation and stationary growth phase. Gene 296, 121128.
  • [9]
    Berche, P., Gaillard, J.L., Richard, S. (1988) Invasiveness and intracellular growth of Listeria monocytogenes. Infection 16 (Suppl. 2), S145S148.
  • [10]
    Conte, M.P., Longhi, C., Petrone, G., Polidoro, M., Valenti, P., Seganti, L. (2000) Modulation of actA gene expression in Listeria monocytogenes by iron. J. Med. Microbiol. 49, 681683.
  • [11]
    Phan-Thanh, L., Gormon, T. (1997) A chemically defined minimal medium for the optimal culture of Listeria. Int. J. Food Microbiol. 35, 9195.
  • [12]
    Archambaud, C., Gouin, E., Pizarro-Cerda, J., Cossart, P., Dussurget, O. (2005) Translation elongation factor EF-Tu is a target for Stp, a serine-threonine phosphatase involved in virulence of Listeria monocytogenes. Mol. Microbiol. 56, 383396.
  • [13]
    Arnaud, M., Chastanet, A., Debarbouille, M. (2004) New vector for efficient allelic replacement in naturally nontransformable, low-GC-content, gram-positive bacteria. Appl. Environ. Microbiol. 70, 68876891.
  • [14]
    Sullivan, M.A., Yasbin, R.E., Young, F.E. (1984) New shuttle vectors for Bacillus subtilis and Escherichia coli which allow rapid detection of inserted fragments. Gene 29, 2126.
  • [15]
    Folio, P., Chavant, P., Chafsey, I., Belkorchia, A., Chambon, C., Hebraud, M. (2004) Two-dimensional electrophoresis database of Listeria monocytogenes EGDe proteome and proteomic analysis of mid-log and stationary growth phase cells. Proteomics 4, 31873201.
  • [16]
    Farr, S.B., Natvig, D.O., Kogoma, T. (1985) Toxicity and mutagenicity of plumbagin and the induction of a possible new DNA repair pathway in Escherichia coli. J. Bacteriol. 164, 13091316.
  • [17]
    Coulanges, V., Andre, P., Ziegler, O., Buchheit, L., Vidon, D.J. (1997) Utilization of iron-catecholamine complexes involving ferric reductase activity in Listeria monocytogenes. Infect. Immun. 65, 27782785.
  • [18]
    Hartford, T., O'Brien, S., Andrew, P.W., Jones, D., Roberts, I.S. (1993) Utilization of transferrin-bound iron by Listeria monocytogenes. FEMS Microbiol. Lett. 108, 311318.
  • [19]
    Deneer, H.G., Boychuk, I. (1993) Reduction of ferric iron by Listeria monocytogenes and other species of Listeria. Can. J. Microbiol. 39, 480485.
  • [20]
    Deneer, H.G., Healey, V., Boychuk, I. (1995) Reduction of exogenous ferric iron by a surface-associated ferric reductase of Listeria spp. Microbiology 141, 19851992.
  • [21]
    Su, M., Cavallo, S., Stefanini, S., Chiancone, E., Chasteen, N.D. (2005) The so-called Listeria innocua ferritin is a Dps protein. Iron incorporation, detoxification, and DNA protection properties. Biochemistry 44, 55725578.
  • [22]
    Ilari, A., Latella, M.C., Ceci, P., Ribacchi, F., Su, M., Giangiacomo, L., Stefanini, S., Chasteen, N.D., Chiancone, E. (2005) The unusual intersubunit ferroxidase center of Listeria innocua Dps is required for hydrogen peroxide detoxification but not for iron uptake. A study with site-specific mutants. Biochemistry 44, 55795587.
  • [23]
    Ilari, A., Ceci, P., Ferrari, D., Rossi, G.L., Chiancone, E. (2002) Iron incorporation into Escherichia coli Dps gives rise to a ferritin-like microcrystalline core. J. Biol. Chem. 277, 3761937623.
  • [24]
    Cooksley, C., Jenks, P.J., Green, A., Cockayne, A., Logan, R.P., Hardie, K.R. (2003) NapA protects Helicobacter pylori from oxidative stress damage, and its production is influenced by the ferric uptake regulator. J. Med. Microbiol. 52, 461469.
  • [25]
    Gupta, S., Chatterji, D. (2003) Bimodal protection of DNA by Mycobacterium smegmatis DNA-binding protein from stationary phase cells. J. Biol. Chem. 278, 52355241.
  • [26]
    Ueshima, J., Shoji, M., Ratnayake, D.B., Abe, K., Yoshida, S., Yamamoto, K., Nakayama, K. (2003) Purification, gene cloning, gene expression, and mutants of Dps from the obligate anaerobe Porphyromonas gingivalis. Infect. Immun. 71, 11701178.
  • [27]
    Ishikawa, T., Mizunoe, Y., Kawabata, S., Takade, A., Harada, M., Wai, S.N., Yoshida, S. (2003) The iron-binding protein Dps confers hydrogen peroxide stress resistance to Campylobacter jejuni. J. Bacteriol. 185, 10101017.
  • [28]
    Ceci, P., Ilari, A., Falvo, E., Chiancone, E. (2003) The Dps protein of Agrobacterium tumefaciens does not bind to DNA but protects it toward oxidative cleavage: X-ray crystal structure, iron binding, and hydroxyl-radical scavenging properties. J. Biol. Chem. 278, 2031920326.
  • [29]
    Yamamoto, Y., Higuchi, M., Poole, L.B., Kamio, Y. (2000) Role of the dpr product in oxygen tolerance in Streptococcus mutans. J. Bacteriol. 182, 37403747.
  • [30]
    Pulliainen, A.T., Haataja, S., Kahkonen, S., Finne, J. (2003) Molecular basis of H2O2 resistance mediated by streptococcal Dpr. Demonstration of the functional involvement of the putative ferroxidase center by site-directed mutagenesis in Streptococcus suis. J. Biol. Chem. 278, 79968005.
  • [31]
    Olsen, K.N., Larsen, M.H., Gahan, C.G., Kallipolitis, B., Wolf, X.A., Rea, R., Hill, C., Ingmer, H. (2005) The Dps-like protein Fri of Listeria monocytogenes promotes stress tolerance and intracellular multiplication in macrophage-like cells. Microbiology 151, 925933.
  • [32]
    Frenkiel-Krispin, D., Levin-Zaidman, S., Shimoni, E., Wolf, S.G., Wachtel, E.J., Arad, T., Finkel, S.E., Kolter, R., Minsky, A. (2001) Regulated phase transitions of bacterial chromatin: a non-enzymatic pathway for generic DNA protection. EMBO J. 20, 11841191.
  • [33]
    Duche, O., Tremoulet, F., Glaser, P., Labadie, J. (2002) Salt stress proteins induced in Listeria monocytogenes. Appl. Environ. Microbiol. 68, 14911498.
  • [34]
    Wouters, J.A., Kamphuis, H.H., Hugenholtz, J., Kuipers, O.P., de Vos, W.M., Abee, T. (2000) Changes in glycolytic activity of Lactococcus lactis induced by low temperature. Appl. Environ. Microbiol. 66, 36863691.
  • [35]
    Behari, J., Youngman, P. (1998) A homolog of CcpA mediates catabolite control in Listeria monocytogenes but not carbon source regulation of virulence genes. J. Bacteriol. 180, 63166324.
  • [36]
    Atichartpongkul, S., Loprasert, S., Vattanaviboon, P., Whangsuk, W., Helmann, J.D., Mongkolsuk, S. (2001) Bacterial Ohr and OsmC paralogues define two protein families with distinct functions and patterns of expression. Microbiology 147, 17751782.
  • [37]
    Bilski, P., Li, M.Y., Ehrenshaft, M., Daub, M.E., Chignell, C.F. (2000) Vitamin B6 (pyridoxine) and its derivatives are efficient singlet oxygen quenchers and potential fungal antioxidants. Photochem. Photobiol. 71, 129134.
  • [38]
    Chumnantana, R., Yokochi, N., Yagi, T. (2005) Vitamin B6 compounds prevent the death of yeast cells due to menadione, a reactive oxygen generator. Biochim. Biophys. Acta 1722, 8491.
  • [39]
    Dufour, A., Voelker, U., Voelker, A., Haldenwang, W.G. (1996) Relative levels and fractionation properties of Bacillus subtilis sigma B and its regulators during balanced growth and stress. J. Bacteriol. 178, 37013709.
  • [40]
    Delumeau, O., Lewis, R.J., Yudkin, M.D. (2002) Protein-protein interactions that regulate the energy stress activation of sigma B in Bacillus subtilis. J. Bacteriol. 184, 55835589.
  • [41]
    Waidner, B., Greiner, S., Odenbreit, S., Kavermann, H., Velayudhan, J., Stahler, F., Guhl, J., Bisse, E., van Vliet, A.H., Andrews, S.C., Kusters, J.G., Kelly, D.J., Haas, R., Kist, M., Bereswill, S. (2002) Essential role of ferritin Pfr in Helicobacter pylori iron metabolism and gastric colonization. Infect. Immun. 70, 39233929.
  • [42]
    Halsey, T.A., Vazquez-Torres, A., Gravdahl, D.J., Fang, F.C., Libby, S.J. (2004) The ferritin-like Dps protein is required for Salmonella enterica serovar Typhimurium oxidative stress resistance and virulence. Infect. Immun. 72, 11551158.