195 resultados para minC


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Analisa e detalha as ações orçamentárias das dotações iniciais constantes da Lei Orçamentária para 2015 – LOA 2015 dos órgãos integrantes da Área Temática IV (Ministério da Ciência, Tecnologia e Inovação – MCTI, Ministério da Educação – MEC, Ministério da Cultura – MinC e Ministério do Esporte – ME) que foram objeto de limitação de movimentação e empenho em face do Decreto nº 8.456, de 22 de maio de 2015.

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

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In Escherichia coli, the Min system, consisting of three proteins, MinC, MinD, and MinE, negatively regulates FtsZ assembly at the cell poles, helping to ensure that the Z ring will assemble only at midcell. Of the three Min proteins, MinC is sufficient to inhibit Z-ring assembly. By binding to MinD, which is mostly localized at the membrane near the cell poles, MinC is sequestered away from the cell midpoint, increasing the probability of Z-ring assembly there. Previously, it has been shown that the two halves of MinC have two distinct functions. The N-terminal half is sufficient for inhibition of FtsZ assembly, whereas the C-terminal half of the protein is required for binding to MinD as well as to a component of the division septum. In this study, we discovered that overproduction of the C-terminal half of MinC (MinC(122-231)) could also inhibit cell division and that this inhibition was at the level of Z-ring disassembly and dependent on MinD. We also found that fusing green fluorescent protein to either the N-terminal end of MinC(122-231), the C terminus of full-length MinC, or the C terminus of MinC(122-231) perturbed MinC function, which may explain why cell division inhibition by MinC(122-231) was not detected previously. These results suggest that the C-terminal half of MinC has an additional function in the regulation of Z-ring assembly.

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