Karen Fulan Discola

Universidade de São Paulo

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Luís Eduardo Soares Netto

Universidade de São Paulo

Marcos Antônio de Oliveira

Universidade Estadual Paulista (Unesp)

B.G. Guimarães

Fundação Oswaldo Cruz

José Renato Rosa Cussiol

Universidade Federal de São Paulo

Bruno Brasil Horta

Universidade de São Paulo

Simone Alves

Hospital de Santa Maria

Andréa Dessen

Institut de Biologie Structurale

Gisele Monteiro

Universidade de São Paulo

José Antonio Bárcena

Instituto Maimónides de Investigación Biomédica de Córdoba

Francisco J. Medrano

Centro de Investigaciones Biológicas Margarita Salas

Cooperative Institutions

Universidade de São Paulo

Centre National de la Recherche Scientifique

Universidade Estadual de Campinas (UNICAMP)

Instituto Butantan

Université Grenoble Alpes

Commissariat à l'Énergie Atomique et aux Énergies Alternatives

CEA Grenoble

Brazilian Biosciences National Laboratory

Institut de Biologie Structurale

Brazilian Center for Research in Energy and Materials

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Reactive cysteine in proteins: Protein folding, antioxidant defense, redox signaling and more

Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology (2006)

Luís Eduardo Soares Netto Marcos Antônio de Oliveira Gisele Monteiro Ana Paula Dias Demasi José Renato Rosa Cussiol

Folding (DSP implementation)

Thiol

10.1016/j.cbpc.2006.07.014

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Citations (148)

Ohr from Xylella fastidiosa in oxidized state

Thiago Gerônimo Pires Alegria Karen Fulan Discola José Renato Rosa Cussiol Marcos Antônio de Oliveira L.E.S. Netto

Xylella fastidiosa

10.2210/pdb4xx2/pdb

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Citations (0)

Structural Aspects of the Distinct Biochemical Properties of Glutaredoxin 1 and Glutaredoxin 2 from Saccharomyces cerevisiae

Journal of Molecular Biology (2008)

Karen Fulan Discola Marcos Antônio de Oliveira José Renato Rosa Cussiol Gisele Monteiro José Antonio Bárcena

Glutaredoxin

10.1016/j.jmb.2008.10.055

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Citations (83)

FtsZ filament capping by MciZ, a developmental regulator of bacterial division

Proceedings of the National Academy of Sciences (2015)

Alexandre W. Bisson‐Filho Karen Fulan Discola Patrícia Castellen Valdir Blasios Alexandre Martins

Significance Division of bacteria is executed by a contractile ring whose cytoskeletal framework is FtsZ (filamentation temperature-sensitive Z), a protein evolutionarily related to eukaryotic tubulin. The FtsZ ring is made of filaments of head-to-tail FtsZ subunits but its architecture and the rules governing its assembly are still poorly known. Here we show that MciZ, an inhibitor of FtsZ ring formation, functions by capping the minus end of FtsZ filaments. Capping by MciZ makes FtsZ filaments shorter than normal, likely by blocking filament annealing; this represents fundamental information to understand how FtsZ filaments grow and shrink, and attain their normal size. The powerful inhibition of Z-ring assembly by MciZ also suggests that an FtsZ ring cannot form from filaments smaller than a certain size.

FtsZ

Filamentation

10.1073/pnas.1414242112

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Citations (69)

The gene ICS3 from the yeast Saccharomyces cerevisiae is involved in copper homeostasis dependent on extracellular pH

Fungal Genetics and Biology (2015)

Claudia Aznar Alesso Karen Fulan Discola Gisele Monteiro

In the yeast Saccharomyces cerevisiae, many genes are involved in the uptake, transport, storage and detoxification of copper. Large scale studies have noted that deletion of the gene ICS3 increases sensitivity to copper, Sortin 2 and acid exposure. Here, we report a study on the Δics3 strain, in which ICS3 is related to copper homeostasis, affecting the intracellular accumulation of this metal. This strain is sensitive to hydrogen peroxide and copper exposure, but not to other tested transition metals. At pH 6.0, the Δics3 strain accumulates a larger amount of intracellular copper than the wild-type strain, explaining the sensitivity to oxidants in this condition. Unexpectedly, sensitivity to copper exposure only occurs in acidic conditions. This can be explained by the fact that the exposure of Δics3 cells to high copper concentrations at pH 4.0 results in over-accumulation of copper and iron. Moreover, the expression of ICS3 increases in acidic pH, and this is correlated with CCC2 gene expression, since both genes are regulated by Rim101 from the pH regulon. CCC2 is also upregulated in Δics3 in acidic pH. Together, these data indicate that ICS3 is involved in copper homeostasis and is dependent on extracellular pH.

Regulon

Strain (injury)

10.1016/j.fgb.2015.06.007

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Citations (6)

Glutaredoxin 2 oxidized structure

Karen Fulan Discola Marcos Antônio de Oliveira José Antonio Bárcena Pablo Porras B.G. Guimarães

Glutaredoxin

10.2210/pdb3d4m/pdb

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Structural characterization of Ohr (Organic Hydroperoxide Resistance Protein) from Xylella fastidiosa in oxidized conformation

thiago Geromino Pires Alegria Karen Fulan Discola José Renato Rosa Cussiol Luís Eduardo Soares Netto

Xylella fastidiosa

Characterization

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Crystallization and preliminary X-ray diffraction analysis of NADPH-dependent thioredoxin reductase I fromSaccharomyces cerevisiae

Acta Crystallographica Section F Structural Biology and Crystallization Communications (2005)

Marcos Antônio de Oliveira Karen Fulan Discola Simone Alves J.A.R.G. Barbosa Francisco J. Medrano

Thioredoxin reductase 1 (Trr1) from Saccharomyces cerevisiae is a member of the family of pyridine nucleotide-disulfide oxidoreductases capable of reducing the redox-active disulfide bond of the cytosolic thioredoxin 1 (Trx1) and thioredoxin 2 (Trx2). NADPH, Trr1 and Trx1 (or Trx2) comprise the thioredoxin system, which is involved in several biological processes, including the reduction of disulfide bonds and response to oxidative stress. Recombinant Trr1 was expressed in Escherichia coli as a His6-tagged fusion protein and purified by nickel-affinity chromatography. The protein was crystallized using the hanging-drop vapour-diffusion method in the presence of PEG 3000 as precipitant after treatment with hydrogen peroxide. X-ray diffraction data were collected to a maximum resolution of 2.4 Å using a synchrotron-radiation source. The crystal belongs to the centred monoclinic space group C2, with unit-cell parameters a = 127.97, b = 135.41, c = 75.81 Å, β = 89.95°. The crystal structure was solved by molecular-replacement methods and structure refinement is in progress.

10.1107/s174430910500758x

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Citations (11)

Structural insights on the efficient catalysis of hydroperoxide reduction by Ohr: Crystallographic and molecular dynamics approaches

PLoS ONE (2018)

Erika Piccirillo Thiago Gerônimo Pires Alegria Karen Fulan Discola José Renato Rosa Cussiol Renato M. Domingos

Organic hydroperoxide resistance (Ohr) enzymes are highly efficient Cys-based peroxidases that play central roles in bacterial response to fatty acid hydroperoxides and peroxynitrite, two oxidants that are generated during host-pathogen interactions. In the active site of Ohr proteins, the conserved Arg (Arg19 in Ohr from Xylella fastidiosa) and Glu (Glu51 in Ohr from Xylella fastidiosa) residues, among other factors, are involved in the extremely high reactivity of the peroxidatic Cys (Cp) toward hydroperoxides. In the closed state, the thiolate of Cp is in close proximity to the guanidinium group of Arg19. Ohr enzymes can also assume an open state, where the loop containing the catalytic Arg is far away from Cp and Glu51. Here, we aimed to gain insights into the putative structural switches of the Ohr catalytic cycle. First, we describe the crystal structure of Ohr from Xylella fastidiosa (XfOhr) in the open state that, together with the previously described XfOhr structure in the closed state, may represent two snapshots along the coordinate of the enzyme-catalyzed reaction. These two structures were used for the experimental validation of molecular dynamics (MD) simulations. MD simulations employing distinct protonation states and in silico mutagenesis indicated that the polar interactions of Arg19 with Glu51 and Cp contributed to the stabilization of XfOhr in the closed state. Indeed, Cp oxidation to the disulfide state facilitated the switching of the Arg19 loop from the closed to the open state. In addition to the Arg19 loop, other portions of XfOhr displayed high mobility, such as a loop rich in Gly residues. In summary, we obtained a high correlation between crystallographic data, MD simulations and biochemical/enzymatic assays. The dynamics of the Ohr enzymes are unique among the Cys-based peroxidases, in which the active site Arg undergoes structural switches throughout the catalytic cycle, while Cp remains relatively static.

Xylella fastidiosa

Catalytic cycle

10.1371/journal.pone.0196918

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Citations (11)

Structural basis of eukaryotic cell targeting by type III secretion system (T3SS) effectors

Research in Microbiology (2013)

T. Tosi A. Pflug Karen Fulan Discola David Neves Andréa Dessen

10.1016/j.resmic.2013.03.019

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Citations (28)