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Ponencias en congresos:
HUPF CONTRIBUTES TO PROTECTION AGAINST OXYGEN DURING HYDROGENASE BIOSYNTHESIS IN RHIZOBIUM LEGUMINOSARUM
Año:2012
Áreas de investigación
  • Biología molecular, celular y genética
Datos
Descripción
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.
Internacional
Si
Nombre congreso
10th European Nitrogen Fixation Conference
Tipo de participación
960
Lugar del congreso
Munich, Alemania
Revisores
Si
ISBN o ISSN
00000-00000
DOI
Fecha inicio congreso
02/09/2012
Fecha fin congreso
05/09/2012
Desde la página
23
Hasta la página
23
Título de las actas
Book of Abstracts
Esta actividad pertenece a memorias de investigación
Participantes
  • Autor: Marta Albareda Contreras (UPM)
  • Autor: Hamid Manyani (ResBioAgro)
  • Autor: Tomas-Andres Ruiz Argueso (UPM)
  • Autor: Juan Imperial Ródenas (UPM)
  • Autor: Luis Fernandez Pacios (UPM)
  • Autor: August Böck (University of Munich)
  • Autor: Jose Manuel Palacios Alberti (UPM)
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