Molecular physiology of nickel and cobalt homeostasis in Rhizobium leguminosarum.

Palacios Alberti, Jose Manuel and Rubio Sanz, Laura and Prieto Carbajo, Rosa Isabel and Menéndez Cerón, M. and Albareda Contreras, Marta and Clavijo, C. and Imperial Ródenas, Juan and Mandrand Berthelot, M. A. and Rodrigue, A. and Cacho, C. del and Ruiz Argüeso, Tomas-Andres and Brito Lopez, Maria Belen (2013). Molecular physiology of nickel and cobalt homeostasis in Rhizobium leguminosarum.. In: "II Conferencia Iberoamericana de Interacciones Beneficiosas MiIcroorganismo-Planta-Ambiente (IBEMPA)", 02/09/2013-06/09/2013, Sevilla.

Description

Title: Molecular physiology of nickel and cobalt homeostasis in Rhizobium leguminosarum.
Author/s:
  • Palacios Alberti, Jose Manuel
  • Rubio Sanz, Laura
  • Prieto Carbajo, Rosa Isabel
  • Menéndez Cerón, M.
  • Albareda Contreras, Marta
  • Clavijo, C.
  • Imperial Ródenas, Juan
  • Mandrand Berthelot, M. A.
  • Rodrigue, A.
  • Cacho, C. del
  • Ruiz Argüeso, Tomas-Andres
  • Brito Lopez, Maria Belen
Item Type: Presentation at Congress or Conference (Article)
Event Title: II Conferencia Iberoamericana de Interacciones Beneficiosas MiIcroorganismo-Planta-Ambiente (IBEMPA)
Event Dates: 02/09/2013-06/09/2013
Event Location: Sevilla
Title of Book: II Conferencia Iberoamericana de Interacciones Beneficiosas MiIcroorganismo-Planta-Ambiente (IBEMPA)
Date: 2013
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

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+ menor que Mn2+ menor que Fe2+ menor que Co2+ menor que Ni2+ menor que Cu2+mayor queZn2+ 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).

More information

Item ID: 29866
DC Identifier: http://oa.upm.es/29866/
OAI Identifier: oai:oa.upm.es:29866
Official URL: http://congreso.us.es/ibempa/index.php/en/preliminary-program/ii-congress-ibempa
Deposited by: Memoria Investigacion
Deposited on: 03 Jul 2014 14:47
Last Modified: 22 Apr 2016 00:13
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