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Descripción
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| Azotobacter vinelandii is a model organism for biochemical studies of N2 fixation that has the peculiarity of being able to fix N2 under aerobic conditions. This process could be carried out via three homologous nitrogenases that differ in the heterometal found at their active sites: the Mo nitrogenase, the V nitrogenase and the Fe-only nitrogenase (1). Expression of either Mo nitrogenase or the alternative nitrogenases depends on the metal availability in the medium, with molybdate acting as co-repressor of alternative nitrogenases. In addition, A. vinelandii carries a molybdenum storage protein, referred to as MoSto, which can store up to 25-fold more Mo than needed during maximum nitrogenase activity (2,3). In this work we investigate a plausible role of MoSto as an obligate intermediate in the Mo trafficking pathway that provides molybdenum for the biosynthesis of the iron-molybdenum cofactor (FeMo-co) of the Mo nitrogenase. We analyze the phenotype of an A. vinelandii mosAB in-frame deletion mutant strain, which lacks the genes encoding the MoSto subunits. Wild type and mutant strains are compared in: (i) their ability to grow diazotrophically and non-diazotrophically in media containing decreasing amounts of molybdate; (ii) their levels of intracellular Mo; (iii) the in vivo levels of Mo nitrogenase activity; (iv) their capacity to repress expression of the alternative nitrogenases. | |
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Internacional
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Si |
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Nombre congreso
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12th European Nitrogen Fixation Conference |
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Tipo de participación
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960 |
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Lugar del congreso
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Budapest |
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Revisores
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Si |
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ISBN o ISSN
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0000000000 |
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DOI
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Fecha inicio congreso
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25/08/2016 |
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Fecha fin congreso
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28/08/2016 |
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Desde la página
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135 |
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Hasta la página
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135 |
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Título de las actas
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12th European Nitrogen Fixation Conference |