Observatorio de I+D+i UPM

Memorias de investigación
Research Publications in journals:
Dual role of HupF in the biosynthesis of [NiFe] hydrogenase in Rhizobium leguminosarum
Year:2012
Research Areas
  • Molecular, cellular and genetic biology
Information
Abstract
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.
International
Si
JCR
Si
Title
Bmc Microbiology
ISBN
1471-2180
Impact factor JCR
3,044
Impact info
Volume
12
doi:10.1186/1471-2180-12-256
Journal number
From page
256
To page
268
Month
SIN MES
Ranking
Participants
  • 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)
Research Group, Departaments and Institutes related
  • Creador: Grupo de Investigación: Asociaciones simbióticas planta-microorganismo
  • Centro o Instituto I+D+i: Centro de Biotecnología y Genómica de Plantas, CBGP
S2i 2020 Observatorio de investigación @ UPM con la colaboración del Consejo Social UPM
Cofinanciación del MINECO en el marco del Programa INNCIDE 2011 (OTR-2011-0236)
Cofinanciación del MINECO en el marco del Programa INNPACTO (IPT-020000-2010-22)