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Memorias de investigación
Communications at congresses:
HUPF CONTRIBUTES TO PROTECTION AGAINST OXYGEN DURING HYDROGENASE BIOSYNTHESIS IN RHIZOBIUM LEGUMINOSARUM
Year:2012
Research Areas
  • Molecular, cellular and genetic biology
Information
Abstract
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.
International
Si
Congress
10th European Nitrogen Fixation Conference
960
Place
Munich, Alemania
Reviewers
Si
ISBN/ISSN
00000-00000
Start Date
02/09/2012
End Date
05/09/2012
From page
23
To page
23
Book of Abstracts
Participants
  • 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)
Research Group, Departaments and Institutes related
  • Creador: Grupo de Investigación: Asociaciones simbióticas planta-microorganismo
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