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Memorias de investigación
Artículos en revistas:
Dual role of HupF in the biosynthesis of [NiFe] hydrogenase in Rhizobium leguminosarum
Año:2012
Áreas de investigación
  • Biología molecular, celular y genética
Datos
Descripción
Background: [NiFe] hydrogenases are enzymes that catalyze the oxidation of hydrogen into protons and electrons, to use H2 as energy source, or the production of hydrogen through proton reduction, as an escape valve for the excess of reduction equivalents in anaerobic metabolism. Biosynthesis of [NiFe] hydrogenases is a complex process that occurs in the cytoplasm, where a number of auxiliary proteins are required to synthesize and insert the metal cofactors into the enzyme structural units. The endosymbiotic bacterium Rhizobium leguminosarum requires the products of eighteen genes (hupSLCDEFGHIJKhypABFCDEX) to synthesize an active hydrogenase. hupF and hupK genes are found only in hydrogenase clusters from bacteria expressing hydrogenase in the presence of oxygen. Results: HupF is a HypC paralogue with a similar predicted structure, except for the C-terminal domain present only in HupF. Deletion of hupF results in the inability to process the hydrogenase large subunit HupL, and also in reduced stability of this subunit when cells are exposed to high oxygen tensions. A ?hupF mutant was fully complemented for hydrogenase activity by a C-terminal deletion derivative under symbiotic, ultra low-oxygen tensions, but only partial complementation was observed in free living cells under higher oxygen tensions (1% or 3%). Co-purification experiments using StrepTag-labelled HupF derivatives and mass spectrometry analysis indicate the existence of a major complex involving HupL and HupF, and a less abundant HupF-HupK complex. Conclusions: The results indicate that HupF has a dual role during hydrogenase biosynthesis: it is required for hydrogenase large subunit processing and it also acts as a chaperone to stabilize HupL when hydrogenase is synthesized in the presence of oxygen.
Internacional
Si
JCR del ISI
Si
Título de la revista
Bmc Microbiology
ISSN
1471-2180
Factor de impacto JCR
3,044
Información de impacto
Volumen
12
DOI
doi:10.1186/1471-2180-12-256
Número de revista
Desde la página
256
Hasta la página
268
Mes
SIN MES
Ranking
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Participantes
  • Autor: Marta Albareda Contreras (UPM)
  • Autor: Hamid Manyani (ResBioAbro)
  • Autor: Maria Belen Brito Lopez (UPM)
  • Autor: Juan Imperial Ródenas (UPM)
  • Autor: Tomas-Andres Ruiz Argueso (UPM)
  • Autor: August Böck (University of Munich)
  • Autor: Jose Manuel Palacios Alberti (UPM)
Grupos de investigación, Departamentos, Centros e Institutos de I+D+i relacionados
  • Creador: Grupo de Investigación: Asociaciones simbióticas planta-microorganismo
  • Centro o Instituto I+D+i: Centro de Biotecnología y Genómica de Plantas, CBGP
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