Peroxiredoxins as cellular guardians in Sulfolobus solfataricus - characterization of Bcp1, Bcp3 and Bcp4(153 visite) Limauro D, Pedone E, Galdi I, Bartolucci S
*** IBB - CNR *** Dipartimento di Biologia Strutturale e Funzionale, Complesso Universitario di Monte S. Angelo, Università di Napoli 'Federico II', Via Cinthia, 80126 Naples, Italy Istituto di Biostrutture e Bioimmagini, CNR, Naples, Italy
Riferimenti:
Imaly, J.A., Pathways of oxidative damage (2003) Annu Rev Microbiol, 57, pp. 395-41
Rho, B.S., Hung, L.W., Holton, J.M., Vigil, D., Kim, S.I., Park, M.S., Terwilliger, T.C., Pedelacq, J.D., Functional and structural characterization of a thiol peroxidase from Mycobacterium tuberculosis (2006) J Mol Biol, 361, pp. 850-863
Jeon, S.J., Ishikawa, K., Characterization of novel hexadecameric thioredoxin peroxidase from Aeropyrum pernix K1 (2003) J Biol Chem, 278, pp. 24174-24180
Dietz, K.J., Jacob, S., Oelze, M.L., Laxa, M., Tognetti, V., De Miranda, S.M., Baier, M., Finkemeier, I., The function of peroxiredoxins in plant organelle redox metabolism (2006) J Exp Bot, 57, pp. 1697-1709
Wood, Z.A., Schroder, E., Robin, H.J., Poole, L.B., Structure, mechanism and regulation of peroxiredoxins (2003) Trends Biochem Sci, 28, pp. 32-40
Seaver, L.C., Imlay, J.A., Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli (2001) J Bacteriol, 183, pp. 7173-7181
Kashima, Y., Ishikawa, K., Alkyl hydroperoxide reductase dependent on thioredoxin-like protein from Pyrococcus horikoshii (2003) J Biochem (Tokyo), 134, pp. 25-29
Kawakami, R., Sakuraba, H., Kamohara, S., Goda, S., Kawarabayasi, Y., Ohshima, T., Oxidative stress response in an anaerobic hyperthermophilic archaeon: Presence of a functional peroxiredoxin in Pyrococcus horikoshii (2004) J Biochem (Tokyo), 136, pp. 541-547
She, Q., Singh, R.K., Confalonieri, F., Zivanovic, Y., Allard, G., Awayez, M.J., Chan-Weiher, C.C., De Moors, A., The complete genome of the crenarchaeon Sulfolobus solfataricus P2 (2001) Proc Natl Acad Sci USA, 98, pp. 7835-7840
Ursby, T., Adinolfi, B.S., Al-Karadaghi, S., De Vendittis, E., Bocchini, V., Iron superoxide dismutase from the archaeon Sulfolobus solfataricus: Analysis of structure and thermostability (1999) J Mol Biol, 286, pp. 189-205
Limauro, D., Pedone, E., Pirone, L., Bartolucci, S., Identification and characterization of 1-Cys peroxiredoxin from Sulfolobus solfataricus and its involvement in the response to oxidative stress (2006) FEBS J, 273, pp. 721-731
De Vendittis, E., Ursby, T., Rullo, R., Gogliettino, M.A., Masullo, M., Bocchini, V., Phenylmethanesulfonyl fluoride inactivates an archaeal superoxide dismutase by chemical modification of a specific tyrosine residue. Cloning, sequencing and expression of the gene coding for Sulfolobus solfataricus superoxide dismutase (2001) Eur J Biochem, 268, pp. 1794-1801
Cannio, R., D'Angelo, A., Rossi, M., Bartolucci, S., A superoxide dismutase from the archaeon Sulfolobus solfataricus is an extracellular enzyme and prevents the deactivation by superoxide of cell-bound proteins (2000) Eur J Biochem, 267, pp. 235-243
Bini, E., Dikshit, V., Dirksen, K., Drozda, M., Blum, P., Stability of mRNA in the hyperthermophilic archaeon Sulfolobus solfataricus (2002) RNA, 8, pp. 1129-1136
Limauro, D., Fiorentino, G., Bartolucci, S., How Sulfolobus responds to enviromental stress (2004) Biochemistry and Molecular Biology in the Thermophilic Archaeon Sulfolobus Solfataricus, pp. 105-130. , In. Farina, B. Faraone Mennella, M.R., eds. pp. Research Signpost, Kerala, India
Pedone, E., D'Ambrosio, K., De Simone, G., Rossi, M., Pedone, C., Bartolucci, S., Insights on a new PDI-like family: Structural and functional analysis of a protein disulfide oxidoreductase from the bacterium Aquifex aeolicus (2006) J Mol Biol, 356, pp. 155-164
Pedone, E., Limauro, D., D'Alterio, R., Rossi, M., Bartolucci, S., Characterization of a multifunctional protein disulfide oxidoreductase from Sulfolobus solfataricus (2006) FEBS J, 273, pp. 5407-5420
Stork, T., Michel, K.P., Pistorius, E.K., Dietz, K.J., Bioinformatic analysis of the genomes of the cyanobacteria Synechocystis sp. PCC 6803 and Synechococcus elongatus PCC 7942 for the presence of peroxiredoxins and their transcript regulation under stress (2005) J Exp Bot, 56, pp. 3193-3206
Copley, S.D., Novak, W.R., Babbitt, P.C., Divergence of function in the thioredoxin fold suprafamily: Evidence for evolution of peroxiredoxins from a thioredoxin-like ancestor (2004) Biochemistry, 43, pp. 13981-13995
Hosoya-Matsuda, N., Motohashi, K., Yoshimura, H., Nozaki, A., Inoue, K., Ohmori, M., Hisabori, T., Anti-oxidative stress system in cyanobacteria. Significance of type II peroxiredoxin and the role of 1-Cys peroxiredoxin in Synechocystis sp. strain PCC 6803 (2005) J Biol Chem, 7, pp. 840-846
Arnold, H.P., She, Q., Phan, H., Stedman, K., Prangishvili, D., Holz, I., Kristjansson, J.K., Zillig, W., The genetic elements pSSVx of the extremely thermophilic crenarchaeon Sulfolobus is a hybrid between a plasmid and a virus (1999) Mol Microbiol, 34, pp. 217-226
Bradford, M., A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal Biochem, 72, pp. 248-254
Weber, K., Pringle, J.R., Osborn, M., Measurement of molecular weight by electrophoresis on SDS-acrylamide gel (1972) Methods Enzymol, 26, pp. 3-27
Lim, Y.S., Cha, M.K., Kim, H.K., Uhm, T.B., Park, J.W., Kim, K., Kim, I.H., Removals of hydrogen peroxide and hydroxyl radical by thiol-specific antioxidant protein as a possible role in vivo (1993) Biochem Biophys Res Commun, 192, pp. 273-280
Sambrook, J., Fritsch, E.F., Maniatis, T., (1989) Molecular Cloning: A Laboratory Manual, 2nd Edn., , Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
Imaly, J. A., Pathways of oxidative damage (2003) Annu Rev Microbiol, 57, pp. 395-41
Rho, B. S., Hung, L. W., Holton, J. M., Vigil, D., Kim, S. I., Park, M. S., Terwilliger, T. C., Pedelacq, J. D., Functional and structural characterization of a thiol peroxidase from Mycobacterium tuberculosis (2006) J Mol Biol, 361, pp. 850-863
Jeon, S. J., Ishikawa, K., Characterization of novel hexadecameric thioredoxin peroxidase from Aeropyrum pernix K1 (2003) J Biol Chem, 278, pp. 24174-24180
Dietz, K. J., Jacob, S., Oelze, M. L., Laxa, M., Tognetti, V., De Miranda, S. M., Baier, M., Finkemeier, I., The function of peroxiredoxins in plant organelle redox metabolism (2006) J Exp Bot, 57, pp. 1697-1709
Wood, Z. A., Schroder, E., Robin, H. J., Poole, L. B., Structure, mechanism and regulation of peroxiredoxins (2003) Trends Biochem Sci, 28, pp. 32-40
Seaver, L. C., Imlay, J. A., Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli (2001) J Bacteriol, 183, pp. 7173-7181
She, Q., Singh, R. K., Confalonieri, F., Zivanovic, Y., Allard, G., Awayez, M. J., Chan-Weiher, C. C., De Moors, A., The complete genome of the crenarchaeon Sulfolobus solfataricus P2 (2001) Proc Natl Acad Sci USA, 98, pp. 7835-7840
Copley, S. D., Novak, W. R., Babbitt, P. C., Divergence of function in the thioredoxin fold suprafamily: Evidence for evolution of peroxiredoxins from a thioredoxin-like ancestor (2004) Biochemistry, 43, pp. 13981-13995
Arnold, H. P., She, Q., Phan, H., Stedman, K., Prangishvili, D., Holz, I., Kristjansson, J. K., Zillig, W., The genetic elements pSSVx of the extremely thermophilic crenarchaeon Sulfolobus is a hybrid between a plasmid and a virus (1999) Mol Microbiol, 34, pp. 217-226
Lim, Y. S., Cha, M. K., Kim, H. K., Uhm, T. B., Park, J. W., Kim, K., Kim, I. H., Removals of hydrogen peroxide and hydroxyl radical by thiol-specific antioxidant protein as a possible role in vivo (1993) Biochem Biophys Res Commun, 192, pp. 273-280
Peroxiredoxins are ubiquitous enzymes that are part of the oxidative stress defense system. In the present study, we identified three peroxiredoxins [bacterioferritin comigratory protein (Bcp)1, Bcp3 and Bcp4] in the genome of the aerobic hyperthermophilic archaeon Sulfolobus solfataricus. Based on the cysteine residues conserved in the deduced aminoacidic sequence, Bcp1 and Bcp4 can be classified as 2-Cys peroxiredoxins and Bcp3 as a 1-Cys peroxiredoxin. A comparative study of the recombinant Bcps produced in Escherichia coli showed that these enzymes protect DNA plasmid from oxidative damage and remove both H2O2 and tert-butyl hydroperoxide, although at different efficiencies. We observed that all of them were particularly thermostable and that peak enzymatic activity fell within the range of the growth temperature of S. solfataricus. Furthermore, we discovered an alternative Bcp reduction system whose composition differs from that of the peroxiredoxin reduction system previously characterized in the aerobic hyperthermophilic archaeon Aeropyrum pernix. Whereas the latter uses the thioredoxin/thioredoxin reductase/NADPH system, this alternative Bcp system is formed of the protein disulfide oxidoreducatase, SSO0192, the thioredoxin reductase, SSO2416, and NADPH. The role of Bcps in oxidative stress was investigated using transcriptional analysis. Different northern blot analysis responses suggested that the Bcp antioxidant system of S. solfataricus can both operate at the constitutive level, with Bcp1 and Bcp4 preventing endogenous peroxide formation, and at the inducible level, with Bcp3 and the already characterized Bcp2 protecting cells from the attack of external peroxides.
Ciccarelli M, Sorriento D, Coscioni E, Iaccarino G, Santulli G * Adrenergic Receptors(13 visite) Endocrinol Of The Heart In Health And Dis (ISSN: 9780-1280311249780128031117), 2016; N/D: 285-315. Impact Factor:0 DettagliEsporta in BibTeXEsporta in EndNote
96 Records (90 escludendo Abstract e Conferenze). Impact factor totale: 356.307 (332.86 escludendo Abstract e Conferenze). Impact factor a 5 anni totale: 385.33 (358.763 escludendo Abstract e Conferenze).
ibb.cnr.it