Differential roles of HypC and HupF proteins for hydrogenase synthesis in Rhizobium leguminosarum.

Albareda Contreras, Marta and Manyani, Hamid and Brito Lopez, Maria Belen and Böck, August and Imperial Ródenas, Juan and Ruiz Argüeso, Tomas-Andres and Palacios Alberti, Jose Manuel (2010). Differential roles of HypC and HupF proteins for hydrogenase synthesis in Rhizobium leguminosarum.. In: "XIII Congreso Internacional de Expresión Gráfica Arquitectónica", 15/06/2011 - 18/06/2011, Zaragoza, España. pp. 181-182.

Description

Title: Differential roles of HypC and HupF proteins for hydrogenase synthesis in Rhizobium leguminosarum.
Author/s:
  • Albareda Contreras, Marta
  • Manyani, Hamid
  • Brito Lopez, Maria Belen
  • Böck, August
  • Imperial Ródenas, Juan
  • Ruiz Argüeso, Tomas-Andres
  • Palacios Alberti, Jose Manuel
Item Type: Presentation at Congress or Conference (Article)
Event Title: XIII Congreso Internacional de Expresión Gráfica Arquitectónica
Event Dates: 15/06/2011 - 18/06/2011
Event Location: Zaragoza, España
Title of Book: Biological Nitrogen Fixation and Plant-Associated Microorganisms
Date: 2010
Subjects:
Faculty: E.T.S.I. Agrónomos (UPM) [antigua denominación]
Department: Biotecnologia [hasta 2014]
Creative Commons Licenses: Recognition - No derivative works - Non commercial

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Abstract

Some diazotrophic bacteria induce [NiFe] hydrogenases to recycle the hydrogen evolved by nitrogenase during the nitrogen fixation process. Biosynthesis of Rhizobium leguminosarum [FeNi] hydrogenase requires a number of accessory proteins (products of hup and hyp genes) that mediate the incorporation of Ni and Fe into the active site. Among them, HypC-paralog HupF and HupK are present in bacteria that synthesize hydrogenase in the presence of oxygen. Hydrogenase activity in mutant strains lacking either hupF or hypC genes was severely reduced, indicating that both proteins are essentials for biosynthesis of hydrogenase. Co-purification of StrepTag labelled variants of HupF and HypC by an affinity chromatography-based approach demonstrated interactions between HupL-HupF and HypC-HupK. Experiments carried out with strains induced for hydrogenase under 3% oxygen tensions indicated that HupF might provide additional stability to HupL under these conditions

More information

Item ID: 9009
DC Identifier: http://oa.upm.es/9009/
OAI Identifier: oai:oa.upm.es:9009
Deposited by: Memoria Investigacion
Deposited on: 05 Oct 2011 08:47
Last Modified: 20 Apr 2016 17:36
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