Artículos de revistas
Heat And Phosphate Starvation Effects On The Proteome, Morphology And Chemical Composition Of The Biomining Bacteria Acidithiobacillus Ferrooxidans
Registro en:
World Journal Of Microbiology And Biotechnology. , v. 27, n. 6, p. 1469 - 1479, 2011.
9593993
10.1007/s11274-010-0599-9
2-s2.0-79955868457
Autor
Ribeiro D.A.
Maretto D.A.
Nogueira F.C.S.
Silva M.J.
Campos F.A.P.
Domont G.B.
Poppi R.J.
Ottoboni L.M.M.
Institución
Resumen
Acidithiobacillus ferrooxidans is a Gram negative, acidophilic, chemolithoautotrophic bacterium that plays an important role in metal bioleaching. During bioleaching, the cells are subjected to changes in the growth temperature and nutrients starvation. The aim of this study was to gather information about the response of the A. ferrooxidans Brazilian strain LR to K2HPO4 starvation and heat stress through investigation of cellular morphology, chemical composition and differential proteome. The scanning electron microscopic results showed that under the tested stress conditions, A. ferrooxidans cells became elongated while the Fourier transform infrared spectroscopy (FT-IR) analysis showed alterations in the wavenumbers between 850 and 1,275 cm-1, which are related to carbohydrates, phospholipids and phosphoproteins. These findings indicate that the bacterial cell surface is affected by the tested stress conditions. A proteomic analysis, using 2-DE and tandem mass spectrometry, enabled the identification of 44 differentially expressed protein spots, being 30 due to heat stress (40°C) and 14 due to K2HPO4 starvation. The identified proteins belonged to 11 different functional categories, including protein fate, energy metabolism and cellular processes. The upregulated proteins were mainly from protein fate and energy metabolism categories. The obtained results provide evidences that A. ferrooxidans LR responds to heat stress and K2HPO4 starvation by inducing alterations in cellular morphology and chemical composition of the cell surface. Also, the identification of several proteins involved in protein fate suggests that the bacteria cellular homesostasis was affected. In addition, the identification of proteins from different functional categories indicates that the A. ferrooxidans response to higher than optimal temperatures and phosphate starvation involves global changes in its physiology. © 2010 Springer Science+Business Media B.V. 27 6 1469 1479 Alvarez, S., Jerez, C.A., Copper ions stimulate polyphosphate degradation and phosphate efflux in Acidithiobacillus ferrooxidans (2004) Appl Environ Microbiol, 70, pp. 5177-5182 Amaro, A.M., Chamorro, D., Seeger, M., Arredondo, R., Peirano, I., Jerez, C.A., Effect of external pH perturbations on in vivo protein synthesis by the acidophilic bacterium Thiobacillus ferrooxidans (1991) J Bacteriol, 173, pp. 910-915 Aoki, H., Dekany, K., Adams, S.L., Ganoza, M.C., The gene encoding the elongation factor P protein is essential for viability and is required for protein synthesis (1997) J Biol Chem, 272, pp. 32254-32259 Beney, L., Gervais, P., Influence of the fluidity of the membrane on the response of microorganisms to environmental stresses (2001) Appl Microbiol Biotechnol, 57, pp. 34-42 Carlos, C., Reis, F.C., Vicentini, R., Madureira, D.J., Ottoboni, L.M.M., The rus operon genes are differentially regulated when Acidithiobacillus ferrooxidans LR is kept in contact with metal sulfides (2008) Curr Microbiol, 57, pp. 375-380 Chalmers, J.M., Griffiths, P.R., (2002) Handbook of Vibrational Spectroscopy, 5. , Chichester: Wiley Cox, J.C., Boxer, D.H., The purification and some properties of rusticyanin, a blue copper protein involved in iron (II) oxidation from Thiobacillus ferrooxidans (1978) Biochem J, 174, pp. 497-502 Eberl, L., Givskov, M., Sternberg, C., Morller, S., Christiansen, G., Molin, S., Physiological responses of Pseudomonas putida KT2442 to phosphate starvation (1996) Microbiol, 142, pp. 51-63 Farah, C., Vera, M., Morin, D., Haras, D., Jerez, C.A., Guiliani, N., Evidence for a functional quorum-sensing type AI-1 system in the extremophilic bacterium Acidithiobacillus ferrooxidans (2005) Appl Environ Microbiol, 71, pp. 7033-7040 Garcia Jr., O., Isolation and purification of Thiobacillus ferrooxidans and Thiobacillus thiooxidans from some coal and uranium mines of Brazil (1991) Braz J Microbiol, 20, pp. 1-6 Hesterkamp, T., Hauser, S., Lutcke, H., Bukau, B., Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains (1996) Proc Natl Acad Sci, 93, pp. 4437-4441 Holmquist, L., Kjelleberg, S., Changes in viability, respiratory activity and morphology of the marine Vibrio sp. strain S14 during starvation of individual nutrients and subsequent recovery (1993) FEMS Microbiol Ecol, 12, pp. 215-224 Hubert, W.A., Leduc, L.G., Ferroni, G.D., Heat and cold shock responses in different strains of Thiobacillus ferrooxidans (1995) Curr Microbiol, 31, pp. 10-14 Jerez, C.A., The heat shock response in meso- and thermoacidophilic chemolithotrophic bacteria (1988) FEMS Microbiol Lett, 56, pp. 289-294 Jerez, C.A., Seeger, M., Amaro, A.M., Phosphate starvation affects the synthesis of outer membrane proteins in Thiobacillus ferrooxidans (1992) FEMS Microbiol Lett, 98, pp. 29-34 Kim, D.Y., Kim, D.R., Ha, S.C., Lokanath, N.K., Lee, C.J., Hwang, H.Y., Kim, K.K., Crystal structure of the protease domain of a heat-shock protein HtrA from Thermotoga maritime (2003) J Biol Chem, 278, pp. 6543-6551 Kitagawa, M., Matsumura, Y., Tsuchido, T., Small heat shock proteins, IbpA and IbpB, are involved in resistances to heat and superoxide stresses in Escherichia coli (2000) FEMS Microbiol Lett, 184, pp. 165-171 Knegt, F.H.P., Mello, L.V., Reis, F.C., Santos, M.T., Vicentini, R., Ferraz, F.C., Ottoboni, L.M.M., ribB and ribBA genes from Acidithiobacillus ferrooxidans: expression levels under different growth conditions and phylogenetic analysis (2008) Res Microbiol, 159, pp. 423-431 Kyrpides, N.C., Woese, C.R., Universally conserved translation initiation factors (1998) Proc Natl Acad Sci USA, 95, pp. 224-228 Laksanalamai, P., Robb, F.T., Small heat shock proteins from extremophiles: a review (2004) Extremophiles, 8, pp. 1-11 Lazar, S., Kolter, R., SurA assists the folding of Escherichia coli outer membrane proteins (1996) J Bacteriol, 178, pp. 1770-1773 Modak, J.M., Natarajan, K.A., Mukhopadhyay, S., Development of temperature-tolerant strains of Thiobacillus ferrooxidans to improve bioleaching kinetics (1996) Hydrometallurgy, 42, pp. 51-61 Pianetti, A., Battistelli, M., Citterio, B., Parlani, C., Falcieri, E., Bruscolini, F., Morphological changes of Aeromonas hydrophila in response to osmotic stress (2009) Micron, 40, pp. 426-433 Rawlings, D.E., Characteristics and adaptability of iron and sulfur-oxidizing microorganisms used for the recovery of metals from minerals and their concentrates (2005) Microb Cell Fact, 4, pp. 1-15 Rilfors, L., Wieslander, A., Stahl, S., Lipid and protein composition of membranes of Bacillus megaterium variants in the temperature range of 5 to 70 degrees C (1978) J Bacteriol, 135, pp. 1043-1052 Seeger, M., Jerez, C.A., Responses of Thiobacillus ferrooxidans to phosphate limitation (1993) FEMS Microbiol Rev, 11, pp. 37-42 Seeger, M., Osorio, G., Jerez, C.A., Phosphorylation of GroEL, DnaK and other proteins from Thiobacillusferrooxidans grown under different conditions (1996) FEMS Microbiol Lett, 138, pp. 129-134 Shi, B., Xia, X., Morphological changes of Pseudomonas pseudoalcaligenes in response to temperature selection (2003) Curr Microbiol, 46, pp. 120-123 Smolka, M.B., Martins, D., Winck, F.V., Santoro, C.E., Castellari, R.R., Ferrari, F., Proteome analysis of the plant pathogen Xylella fastidiosa reveals major cellular and extracellular proteins and a peculiar codon bias distribution (2003) Proteomics, 3, pp. 224-237 Tuovinen, O.H., Kelly, D.P., Biology of Thiobacillus ferrooxidans in relation to the microbiological leaching of sulphide ores (1972) Z Allg Mikrobiol, 12, pp. 311-346 Valdes, J., Pedroso, I., Quatrini, R., Dodson, R.J., Tettelin, H., Blake II, R., Eisen, J.A., Holmes, D.S., Acidithiobacillus ferrooxidans metabolism: from genome sequence to industrial applications (2008) BMC Genomics, 9, pp. 597-621 van der Veen, S., van Schalkwijk, S., Molenaar, D., de Vos, W., Abee, T., Wells-Bennik, M.H.J., The SOS response of Listeria monocytogenes is involved in stress resistance and mutagenesis (2010) Microbiol, 156, pp. 374-384 Vasconcelos, A.R., Nogueira, F.C.S., Abreu, E.F.M., Gonçalves, E.F.P., Souza, A.S., Campos, F.A.P., Protein extraction from cowpea tissues for 2D electrophoresis and MS analysis (2005) Chromatographia, 62, pp. 447-450 Wang, Y., Zhang, X., Liu, Q., Ai, C., Mo, H., Zeng, J., Expression, purification and molecular structure modeling of thioredoxin (Trx) and thioredoxin reductase (TrxR) from Acidithiobacillus ferrooxidans (2009) Curr Microbiol, 59, pp. 35-41 Xiao, S., Chao, J., Wang, W., Fang, F., Qiu, G., Liu, X., Real-time PCR analysis of the heat-shock response of Acidithiobacillus ferrooxidans ATCC 23270 (2009) Folia Biol, 55, pp. 1-6 Yarzábal, A., Duquesne, K., Bonnefoy, V., Rusticyanin gene expression of Acidithiobacillus ferrooxidans ATCC 33020 in sulfur- and in ferrous iron media (2003) Hydrometallurgy, 71, pp. 107-114 Yu, C., Irudayaraj, J., Spectroscopic characterization of microorganisms by Fourier transform infrared microspectroscopy (2004) Biopolymers, 77, pp. 368-377