Observatorio de I+D+i UPM

Memorias de investigación
Conferencias:
Molecular physiology of nickel and cobalt homeostasis in Rhizobium leguminosarum.
Año:2013
Áreas de investigación
  • Microbiología
Datos
Descripción
Transition metals such as Fe, Cu, Mn, Ni, or Co are essential nutrients, as they are constitutive elements of a significant fraction of cell proteins. Such metals are present in the active site of many enzymes, and also participate as structural elements in different proteins. From a chemical point of view, metals have a defined order of affinity for binding, designated as the Irving-Williams series (Irving and Williams, 1948) Mg2+ < Mn2+ < Fe2+ < Co2+ < Ni2+ < Cu2+>Zn2+ Since cells contain a high number of different proteins harbouring different metal ions, a simplistic model in which proteins are synthesized and metals imported into a ?cytoplasmic soup? cannot explain the final product that we find in the cell. Instead we need to envisage a complex model in which specific ligands are present in definite amounts to leave the right amounts of available metals and protein binding sites, so specific pairs can bind appropriately. A critical control on the amount of ligands and metal present is exerted through specific metal-responsive regulators able to induce the synthesis of the right amount of ligands (essentially metal binding proteins), import and efflux proteins. These systems are adapted to establish the metal-protein equilibria compatible with the formation of the right metalloprotein complexes. Understanding this complex network of interactions is central to the understanding of metal metabolism for the synthesis of metalloenzymes, a key topic in the Rhizobium-legume symbiosis. In the case of the Rhizobium leguminosarum bv viciae (Rlv) UPM791 -Pisum sativum symbiotic system, the concentration of nickel in the plant nutrient solution is a limiting factor for hydrogenase expression, and provision of high amounts of this element to the plant nutrient solution is required to ensure optimal levels of enzyme synthesis (Brito et al., 1994).
Internacional
Si
ISSN o ISBN
0000-0000
Entidad relacionada
Nacionalidad Entidad
Sin nacionalidad
Lugar del congreso
Sevilla
Esta actividad pertenece a memorias de investigación
Participantes
  • Autor: Jose Manuel Palacios Alberti (UPM)
  • Autor: Laura Rubio Sanz (UPM)
  • Autor: Tomas-Andres Ruiz Argueso (UPM)
  • Autor: Marta Albareda Contreras (UPM)
  • Autor: Juan Imperial Ródenas (UPM)
  • Autor: Mrie-Andree Mandrand Berthelot (Universidad de Lyon)
  • Autor: Agnes Rodrigue (Universidad de Lyon)
  • Autor: Mariana Menendez Ceron (Universidad Politecnica de Madrid)
  • Autor: Carlos Clavijo (Univerisidad Politecnica de Madrid)
  • Autor: Carmen Cacho Vicente (IHCP JCR, Ispra)
  • Autor: Rosa Isabel Prieto Carbajo (Universidad Politécnica de Madrid)
  • Autor: Maria Belen Brito Lopez (UPM)
Grupos de investigación, Departamentos, Centros e Institutos de I+D+i relacionados
  • Creador: Grupo de Investigación: Asociaciones simbióticas planta-microorganismo
  • Departamento: Química y Análisis Agrícola
  • Departamento: Biotecnología
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