The structural molecular biology network of the State of São Paulo, Brazil

This article describes the achievements of the Structural Molecular Biology Network (SMolBNet), a collaborative program of structural molecular biology, centered in the State of São Paulo, Brazil, and supported by São Paulo State Funding Agency (FAPESP). It gathers twenty scientific groups and is coordinated by the scientific staff of the Center of Structural Molecular Biology, at the National Laboratory of Synchrotron Light (LNLS), in Campinas. The SMolBNet program has been aimed at 1) solving the structure of proteins of interest related to the research projects of the groups. In some cases, the choice has been to select proteins of unknown function or of possible novel structure obtained from the sequenced genomes of the FAPESP genomic program; 2) providing the groups with training in all the steps of the protein structure determination: gene cloning, protein expression, protein purification, protein crystallization and structure determination. Having begun in 2001, the program has been successful in both aims. Here, four groups reveal their participation in the program and describe the structural aspects of the proteins they have selected to study.Esse artigo descreve realizações do Programa SMolBNet (Rede de Biologia Molecular Estrutural) do Estado de São Paulo, apoiado pela FAPESP (Fundação de Apoio à Pesquisa do Estado de São Paulo). Ele reúne vinte grupos de pesquisa e é coordenado pelos pesquisadores do Laboratório Nacional de Luz Síncrotron (LNLS), em Campinas. O Programa SMolBNet tem como metas: Elucidar a estrutura tridimensional de proteínas de interesse aos grupos de pesquisa componentes do Programa; Prover os grupos com treinamento em todas as etapas de determinação de estrutura: clonagem gênica, expressão de proteínas, purificação de proteínas, cristalização de proteínas e elucidação de suas estruturas. Tendo começado em 2001, o Programa alcançou sucesso em ambas as metas. Neste artigo, quatro dos grupos descrevem suas participações, e discutem aspectos estruturais das proteínas que eles selecionaram para estudos.Centro de Biologia Molecular Estrutural Laboratório Nacional de Luz SíncrotronUniversidade de São Paulo Instituto de Biociências Departamento de Genética e Processos EvolutivosUniversidade de São Paulo Instituto de Química Departamento de BioquímicaUniversidade Federal de São Paulo (UNIFESP) Escola Paulista de MedicinaCentro Latino-Americano e do Caribe de Informação em Ciências da Saúde BIREMEUNIFESP, EPMSciEL

Characteristcs chemical and soil salinization in the Irrigated District of California, SE, Brazil

O manejo inadequado da irrigação pode resultar no acúmulo de sais no solo, cuja intensidade depende da qualidade da água utilizada na irrigação, da fração de lixiviação adotada e da demanda evapotranspirativa da região. O presente trabalho teve como objetivo avaliar os atributos físicos e químicos dos solos do perímetro irrigado Califórnia, localizado no extremo noroeste do Estado de Sergipe. Para tal, foram realizadas amostragens em 42 lotes, correspondendo a 16,4% dos lotes deste perímetro. As maiores concentrações de sais e de sódio ocorreram na camada superficial (0–0,2m) do solo, o que evidenciou a falta de um manejo da irrigação adequado visando ao controle da salinidade. O aumento do pH do solo foi correlacionado significativamente com a porcentagem de sódio trocável, atingindo valores acima de 9,5. Correlações positivas significativas foram observadas entre a condutividade elétrica e os teores de Ca e Mg, indicando que sais desses íons podem estar se acumulando no solo pela ascensão do lençol freático, associado à ausência de lixiviação e drenagem. _________________________________________________________________________________________ ABSTRACT: The improper irrigation management may result in the accumulation of salts in the soil profile, which intensity depends on the irrigation water quality, the leaching fraction adopted and on the evapotranspiration demand of the region. The objective of the present study was to study the physical and chemical characteristics of the soils in the irrigated district of California, located in the northwest of the State of Sergipe. Thus, soil sampling were made in 54 lots, corresponding to 16.4% of the lots of this district. The highest salt and sodium concentrations occurred in the shallowest soil layer (0–0.2m), evidencing the lack of an appropriate irrigation management in order to control the salinity build up. The increasing of the soil pH was significantly correlated to the exchangeable sodium percentage, reaching values over 9.5. Significant positive correlations were observed between the electrical conductivity and the Ca and Mg content, indicating that salts of both ions could be accumulating in soil by the capillary rise of the water table, associated to the lack of leaching and drainage

Redox activation of Nox1 (NADPH Oxidase 1) involves an intermolecular disulfide bond between protein disulfide isomerase and p47phox in vascular smooth muscle cells

Objective— PDI (protein disulfide isomerase A1) was reported to support Nox1 (NADPH oxidase) activation mediated by growth factors in vascular smooth muscle cells. Our aim was to investigate the molecular mechanism by which PDI activates Nox1 and the functional implications of PDI in Nox1 activation in vascular disease. Approach and Results— Using recombinant proteins, we identified a redox interaction between PDI and the cytosolic subunit p47phox in vitro. Mass spectrometry of crosslinked peptides confirmed redox-dependent disulfide bonds between cysteines of p47phox and PDI and an intramolecular bond between Cys 196 and 378 in p47phox. PDI catalytic Cys 400 and p47phox Cys 196 were essential for the activation of Nox1 by PDI in vascular smooth muscle cells. Transfection of PDI resulted in the rapid oxidation of a redox-sensitive protein linked to p47phox, whereas PDI mutant did not promote this effect. Mutation of p47phox Cys 196, or the redox active cysteines of PDI, prevented Nox1 complex assembly and vascular smooth muscle cell migration. Proximity ligation assay confirmed the interaction of PDI and p47phox in murine carotid arteries after wire injury. Moreover, in human atheroma plaques, a positive correlation between the expression of PDI and p47phox occurred only in PDI family members with the a′ redox active site. Conclusions— PDI redox cysteines facilitate Nox1 complex assembly, thus identifying a new mechanism through which PDI regulates Nox activity in vascular diseas