Análise da legitimidade sociopolítica e cognitiva da controladoria no Brasil

Em diferentes partes do mundo têm sido realizados esforços na busca de legitimidade e identidade para a controladoria, a partir deste contexto emerge a pergunta de pesquisa: Qual a identidade da disciplina Controladoria no Brasil? Para responder esta pergunta, a presente pesquisa baseia-se nos estudos sobre legitimidade e tem como objetivo identificar e analisar a legitimidade sociopolítica (Zimmerman & Zeitz, 2002; Aldrich, 1999) e cognitiva (Scott, 2001; Zimmerman & Zeitz, 2002) da controladoria no Brasil. Para atingir o objetivo proposto, em relação à legitimidade sociopolítica, foram pesquisados documentos, normas e resoluções de órgãos oficiais e de representação de classe, e com a finalidade de analisar a legitimidade cognitiva, as publicações nas principais revistas de contabilidade, congressos e seminários, disciplinas de controladoria, livros e manuais. Os resultados mostram que a controladoria no Brasil apresenta legitimidade sociopolítica, ou seja, possui organismos e normas próprias, contudo, necessita melhorar os níveis de organização e desenvolvimento, assim como ocorre nos Estados Unidos e Alemanha. Observa-se também que a legitimidade cognitiva cresceu na publicação de livros e manuais, a disciplina de controladoria está presente na maioria dos cursos de Ciências Contábeis, e apresenta oportunidades de aperfeiçoamento, principalmente no que se refere a publicações em periódicos

Electron transport pathways in isolated chromoplasts from Narcissus pseudonarcissus L

International audienceDuring daffodilflower development,chloroplasts differentiate into photosynthetically inactive chromoplasts, which have lostfunctional photosynthetic reaction centers. Chromoplasts exhibit a respiratory activity reducing oxygen to water and generating ATP. Immunoblots revealed the presence of the plastid terminal oxidase(PTOX), the NAD(P)H dehydrogenase (NDH) complex, the cytochrome b6fcomplex, ATP synthase and several isoforms of ferredoxin-NADP+oxidoreductase (FNR) and of ferredoxin (Fd). Fluorescence spectroscopy allowed the detection of chlorophyll a in the cytochrome b6fcomplex. Here we characterize the electron transport pathway of chromorespiration by using specific inhibitors forthe NDH complex, the cytochrome b6fcomplex, FNR and redox-inactive Fd in which the iron was replaced by gallium. Our data suggest anelectron flowvia twoseparatepathways, both reducing plastoquinone and using PTOX as oxidase. The first oxidizes NADPH via FNR, Fd,and cytochrome bh of the cytochrome b6fcomplex and does not result in the pumpingofprotons across the membrane. In the second,electron transport takes place via the NDH complex using preferentially NADH but also NADPH as electron donor. FNR and Fd are not involved in this pathway. The NDH-complex is responsible for the generation of the proton gradient. We propose a new model for chromorespiration which may also be relevant for the understanding of chlororespiration and for the characterization of the electron input from Fd to the cytochrome b6fcomplex during cyclic electron transport in chloroplasts

Detection of protein–protein interactions at the septin collar in Saccharomyces cerevisiae

Various methods can provide a readout of the physical interaction between two biomolecules. A recently described tripartite split-GFP system has the potential to report by direct visualization via a fluorescence signal the intimate association of minimally tagged proteins expressed at their endogenous level in their native cellular milieu and can capture transient or weak interactions. Here we document the utility of this tripartite split-GFP system to assess in living cells protein–protein interactions in a dynamic cytoskeletal structure—the septin collar at the yeast bud neck. We show, first, that for septin–septin interactions, this method yields a robust signal whose strength reflects the known spacing between the subunits in septin filaments and thus serves as a “molecular ruler.” Second, the method yields little or no spurious signal even with highly abundant cytosolic proteins readily accessible to the bud neck (including molecular chaperone Hsp82 and glycolytic enzyme Pgk1). Third, using two proteins (Bni5 and Hsl1) that have been shown by other means to bind directly to septins at the bud neck in vivo, we validate that the tripartite split-GFP method yields the same conclusions and further insights about specificity. Finally, we demonstrate the capacity of this approach to uncover additional new information by examining whether three other proteins reported to localize to the bud neck (Nis1, Bud4, and Hof1) are able to interact physically with any of the subunits in the septin collar and, if so, with which ones