Browsing by Author "Lagos Mónaco, Rosalba"

Now showing items 1-10 of 10

    • 4',6-Diamidino-2-phenylindole (DAPI) induces bundling of Escherichia coli FtsZ polymers inhibiting the ... 
      Nova Martínez, Esteban; Montecinos, Felipe; Brunet, Juan E.; Lagos Mónaco, Rosalba; Monasterio Opazo, Octavio (ELSEVIER SCIENCE INC, 2007-09-15)
      FtsZ (Filamentous temperature sensitivity Z) cell division protein from Escherichia coli binds the fluorescence probe DAPI. Bundling of FtsZ was facilitated in the presence of DAPI, and the polymers in solution remained ...
    • Amyloid formation modulates the biological activity of a bacterial protein 
      Bieler, Sylvain; Estrada, Lisbell D.; Lagos Mónaco, Rosalba; Baeza Cancino, Marcelo; Castilla, Joaquín; Soto, Claudio (AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 2005-07-22)
      The aggregation of proteins into amyloid fibrils is the hallmark feature of a group of late-onset degenerative diseases including Alzheimer, Parkinson, and prion diseases. We report here that microcin E492, a peptide ...
    • Antibacterial and antitumorigenic properties of microcin E492, a poreforming bacteriocin 
      Lagos Mónaco, Rosalba; Tello,; Mercado,; García,; Monasterio Opazo, Octavio (2009)
      Microcins are a family of low-molecular weight bacteriocins produced and secreted by Gram-negative bacteria. This review is focused on microcin E492, a pore-forming bacteriocin produced by Klebsiella pneumoniae RYC492 that ...
    • Domain folding and flexibility of Escherichia coli FtsZ determined by tryptophan site-directed mutagenesis 
      Díaz Espinoza, Rodrigo; Garcés, Andrea P.; Arbildua, José J.; Montecinos, Felipe; Brunet, Juan E.; Lagos Mónaco, Rosalba; Monasterio Opazo, Octavio (COLD SPRING HARBOR LAB PRESS, 2007-08)
      FtsZ has two domains, the amino GTPase domain with a Rossmann fold, and the carboxyl domain that resembles the chorismate mutase fold. Bioinformatics analyses suggest that the interdomain interaction is stronger than the ...
    • Fluorescence resonance energy transfer and molecular modeling studies on 4 ',6-diamidino-2-phenylindole ... 
      Arbildua, José J.; Brunet, Juan E.; Jameson, David M.; López, Maribel; Nova Martínez, Esteban; Lagos Mónaco, Rosalba; Monasterio Opazo, Octavio (COLD SPRING HARBOR LAB PRESS, 2006-03)
      The goal of this work was to determine the binding properties and location of 4',6-diamidino-2-phenyl=indole (DAPI) complexed with tubulin. Using fluorescence anisotropy, a dissociation constant of 5.2 +/- 0.4 mu M for the ...
    • Identification of Key Amino Acid Residues Modulating Intracellular and In vitro Microcin E492 Amyloid Formation 
      Aguilera, Paulina; Marcoleta Caldera, Andrés; Lobos Ruiz, Pablo; Arranz, Rocío; Valpuesta, José M.; Monasterio Opazo, Octavio; Lagos Mónaco, Rosalba (Frontiers Media S.A., 2016)
      Microcin E492 (MccE492) is a pore-forming bacteriocin produced and exported by Klebsiella pneumoniae RYC492. Besides its antibacterial activity, excreted MccE492 can form amyloid fibrils in vivo as well as in vitro. It has ...
    • Microcin E492 Amyloid Formation Is Retarded by Posttranslational Modification 
      Marcoleta, Andrés; Marín, Macarena; Mercado, Gabriela; Valpuesta, José María; Monasterio Opazo, Octavio; Lagos Mónaco, Rosalba (American Society for Microbiology, 2013)
      Microcin E492, a channel-forming bacteriocin with the ability to form amyloid fibers, is exported as a mixture of two forms: unmodified (inactive) and posttranslationally modified at the C terminus with a salmochelin-like ...
    • The production in vivo of microcin E492 with antibacterial activity depends on salmochelin and EntF 
      Mercado, Gabriela; Tello, Mario; Marín, Macarena; Monasterio Opazo, Octavio; Lagos Mónaco, Rosalba (AMER SOC MICROBIOLOGY, 2008-08)
      Microcin E492 is a channel-forming bacteriocin that is found in two forms, namely, a posttranslationally modified form obtained by the covalent linkage of salmochelin-like molecules to serine 84 and an unmodified form. ...
    • Single tryptophan mutants of FtsZ: Nucleotide binding/exchange and conformational transitions 
      Montecinos Franjola, Felipe Antonio; James, Nicholas G.; Concha Marambio, Luis; Brunet, Juan E.; Lagos Mónaco, Rosalba; Monasterio Opazo, Octavio; Jameson, David M. (Elsevier, 2014)
      Cell division protein FtsZ cooperatively self-assembles into straight filaments when bound to GTP. A set of conformational changes that are linked to FtsZ GTPase activity are involved in the transition from straight to ...
    • Studies on the Dissociation and Urea-Induced Unfolding of FtsZ Support the Dimer Nucleus Polymerization Mechanism 
      Montecinos Franjola, Felipe; Ross, Justin A.; Sánchez, Susana A.; Brunet, Juan E.; Lagos Mónaco, Rosalba; Jameson, David M.; Monasterio Opazo, Octavio (2012-05)
      FtsZ is a major protein in bacterial cytokinesis that polymerizes into single filaments. A dimer has been proposed to be the nucleating species in FtsZ polymerization. To investigate the influence of the self-assembly of ...