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  • ÍtemAcceso Abierto
    A long-chain flavodoxin protects pseudomonas aeruginosa from oxidative stress and host bacterial clearance
    (Public Library of Science (PLOS), 2014-02-13) Moyano, Alejandro José; Tobares, Romina Alín; Rizzi, Yanina S.; Krapp, Adriana R.; Mondotte, Juan Alberto; Bocco, José Luis; Saleh, Maria-Carla; Carrillo, Néstor; Smania, Andrea M.
    Long-chain flavodoxins, ubiquitous electron shuttles containing flavin mononucleotide (FMN) as prosthetic group, play an important protective role against reactive oxygen species (ROS) in various microorganisms. Pseudomonas aeruginosa is an opportunistic pathogen which frequently has to face ROS toxicity in the environment as well as within the host. We identified a single ORF, hereafter referred to as fldP (for flavodoxin from P. aeruginosa), displaying the highest similarity in length, sequence identity and predicted secondary structure with typical long-chain flavodoxins. The gene was cloned and expressed in Escherichia coli. The recombinant product (FldP) could bind FMN and exhibited flavodoxin activity in vitro. Expression of fldP in P. aeruginosa was induced by oxidative stress conditions through an OxyR-independent mechanism, and an fldP-null mutant accumulated higher intracellular ROS levels and exhibited decreased tolerance to H2O2 toxicity compared to wild-type siblings. The mutant phenotype could be complemented by expression of a cyanobacterial flavodoxin. Overexpression of FldP in a mutT-deficient P. aeruginosa strain decreased H2O2-induced cell death and the hypermutability caused by DNA oxidative damage. FldP contributed to the survival of P. aeruginosa within cultured mammalian macrophages and in infected Drosophila melanogaster, which led in turn to accelerated death of the flies. Interestingly, the fldP gene is present in some but not all P. aeruginosa strains, constituting a component of the P. aeruginosa accessory genome. It is located in a genomic island as part of a self-regulated polycistronic operon containing a suite of stress-associated genes. The collected results indicate that the fldP gene encodes a long-chain flavodoxin, which protects the cell from oxidative stress, thereby expanding the capabilities of P. aeruginosa to thrive in hostile environments.
  • ÍtemAcceso Abierto
    Transcriptional and Metabolic Changes Associated to the Infection by Fusarium verticillioides in Maize Inbreds with Contrasting Ear Rot Resistance
    (Public Library of Science, 2013-04-18) Campos Bermudez, Valeria A.; Fauguel, Carolina M.; Tronconi, Marcos A.; Casati, Paula; Presello, Daniel A.; Andreo, Carlos S.
    Fusarium verticillioides causes ear rot and grain mycotoxins in maize (Zea mays L.), which are harmful to human and animal health. Breeding and growing less susceptible plant genotypes is one alternative to reduce these detrimental effects. A better understanding of the resistance mechanisms would facilitate the implementation of strategic molecular agriculture to breeding of resistant germplasm. Our aim was to identify genes and metabolites that may be related to the Fusarium reaction in a resistant (L4637) and a susceptible (L4674) inbred. Gene expression data were obtained from microarray hybridizations in inoculated and non-inoculated kernels from both inbreds. Fungal inoculation did not produce considerable changes in gene expression and metabolites in L4637. Defense-related genes changed in L4674 kernels, responding specifically to the pathogen infection. These results indicate that L4637 resistance may be mainly due to constitutive defense mechanisms preventing fungal infection. These mechanisms seem to be poorly expressed in L4674; and despite the inoculation activate a defense response; this is not enough to prevent the disease progress in this susceptible line. Through this study, a global view of differential genes expressed and metabolites accumulated during resistance and susceptibility to F. verticillioides inoculation has been obtained, giving additional information about the mechanisms and pathways conferring resistance to this important disease in maize.
  • ÍtemAcceso Abierto
    Engineering Climate-Change-Resilient Crops: New Tools and Approaches
    (MDPI, 2021-07-23) Shahinnia, Fahimeh; Carrillo, Néstor; Hajirezaei, Mohammad-Reza
  • ÍtemAcceso Abierto
    CuA-based chimeric T1 copper sites allow for independent modulation of reorganization energy and reduction potential
    (Royal Society of Chemistry, 2021-02-04) Szuster, Jonathan; Zitare, Ulises A.; Castro, María A.; Leguto, Alcides J.; Morgada, Marcos Nicolás; Vila, Alejandro J.; Murgida, Daniel H.
  • ÍtemAcceso Abierto
    Environmental selection pressures related to iron utilization are involved in the loss of the flavodoxin gene from the plant genome
    (Oxford University Press, 2015-02-16) Pierella Karlusich, Juan J.; Ceccoli, Romina Denis; Graña, Martín; Romero, Héctor; Carrillo, Néstor
  • ÍtemAcceso Abierto
    The heme uptake process in Trypanosoma cruzi epimastigotes is inhibited by heme analogues and by inhibitors of ABC transporters
    (Elsevier, 2011) Cupello Peixoto, Mauricio; Fernandes de Souza, Cíntia; Buchensky, Celeste; Rocha Corrêa Soares, Juliana Baptista; Travassos Laranja, Gustavo Augusto; Garcia Pinto Coelho, Marsen; Cricco, Julia Alejandra; Paes, Marcia Cristina
  • ÍtemAcceso Abierto
    Heme A synthesis and CcO activity are essential for Trypanosoma cruzi infectivity and replication
    (Portland Press, 2017-06-27) Merli, Marcelo Luciano; Cirulli, Brenda Analía; Menéndez-Bravo, Simón M.; Cricco, Julia Alejandra
  • ÍtemAcceso Abierto
    Biosynthesis of heme O in intraerythrocytic stages of Plasmodium falciparum and potential inhibitors of this pathway
    (Springer Nature, 2019-12-17) Simão-Gurge, Raquel M.; Wunderlich, Gerhard; Cricco, Julia Alejandra; Galindo Cubillos, Eliana F.; Domenech-Carbó, Antonio; Cebrián-Torrejón, Gerardo; Almeida, Fernando G.; Cirulli, Brenda Analía; Katzin, Alejandro M.
  • ÍtemAcceso Abierto
    The Trypanosoma cruzi Protein TcHTE Is Critical for Heme Uptake
    (Public Library of Science PLOS, 2016-01) Merli, Marcelo Luciano; Pagura, Lucas; Hernández, Josefina; Barisón, María Julia; Pral, Elizabeth M. F.; Silber, Ariel M.; Cricco, Julia Alejandra
  • ÍtemAcceso Abierto
    Role of Heme and Heme-Proteins in Trypanosomatid essential metabolic pathways
    (Hindawi, 2011) Tripodi, Karina E. J.; Menendez Bravo, Simón M.; Cricco, Julia Alejandra
  • ÍtemAcceso Abierto
    The Trypanosoma cruzi proteins TcCox10 and TcCox15 catalyze the formation of heme A in the yeast Saccharomyces cerevisiae
    (Oxford University Press, 2010-11) Buchensky, Celeste; Almirón, Paula; Suarez Mantilla, Brian; Silber, Ariel M.; Cricco, Julia Alejandra