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Descripción
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| In this work we have studied the role of HupF in hydrogenase synthesis. HupF is a HypC paralogue with an additional C-terminal domain. Co-purification experiments using a StrepTag-labelled variant of R. leguminosarum HupF demonstrated the existence of a HupF-HupL complex. This is consistent with the involvement of this protein in the transfer of NiFe cofactor from HupK into HupL proposed for the Ralstonia eutropha system (Ludwig et al., 2009). Molecular modelling of the R. leguminosarum HupL-HupF complex suggests that the C-terminal domain of HupF is relevant for this interaction. This region is required for full hydrogenase activity in free- living cells grown under microaerobic conditions (1% O2), but is dispensable under the ultra- low oxygen tensions present in the nodule. Furthermore, a R. leguminosarum mutant lacking hupF shows a reduced stability of hydrogenase structural protein HupL when cells are incubated in the presence of high oxygen tensions. These data indicate that the formation of the HupF-HupL complex has a protective role of HupL against inactivation by oxygen during the biosynthetic process. | |
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Internacional
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Si |
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Nombre congreso
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10th 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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Munich, Alemania |
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Revisores
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Si |
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ISBN o ISSN
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00000-00000 |
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DOI
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Fecha inicio congreso
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02/09/2012 |
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Fecha fin congreso
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05/09/2012 |
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Desde la página
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23 |
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Hasta la página
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23 |
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Título de las actas
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Book of Abstracts |