Rhizobium leguminosarum HupE is a highly-specific diffusion facilitator for nickel uptake

Albareda Contreras, Marta and Rodrigue, A. and Brito Lopez, Maria Belen and Ruiz Argüeso, Tomas-Andres and Imperial Ródenas, Juan and Mandar Berthelot, Marie Andree and Palacios Alberti, Jose Manuel (2015). Rhizobium leguminosarum HupE is a highly-specific diffusion facilitator for nickel uptake. "Metallomics", v. 7 ; pp. 691-701. ISSN 1756-5901. https://doi.org/10.1039/C4MT00298A.

Description

Title: Rhizobium leguminosarum HupE is a highly-specific diffusion facilitator for nickel uptake
Author/s:
  • Albareda Contreras, Marta
  • Rodrigue, A.
  • Brito Lopez, Maria Belen
  • Ruiz Argüeso, Tomas-Andres
  • Imperial Ródenas, Juan
  • Mandar Berthelot, Marie Andree
  • Palacios Alberti, Jose Manuel
Item Type: Article
Título de Revista/Publicación: Metallomics
Date: 2015
ISSN: 1756-5901
Volume: 7
Subjects:
Faculty: E.T.S.I. Agrónomos (UPM) [antigua denominación]
Department: Biotecnología - Biología Vegetal
Creative Commons Licenses: Recognition - No derivative works - Non commercial

Full text

[img]
Preview
PDF - Requires a PDF viewer, such as GSview, Xpdf or Adobe Acrobat Reader
Download (1MB) | Preview

Abstract

Bacteria require nickel transporters for the synthesis of Ni-containing metalloenzymes in natural, low nickel habitats. In this work we carry out functional and topological characterization of Rhizobium leguminosarum HupE, a nickel permease required for the provision of this element for [NiFe] hydrogenase synthesis. Expression studies in the Escherichia coli nikABCDE mutant strain HYD723 revealed that HupE is a medium-affinity permease (apparent Km 227 ! 21 nM; Vmax 49 ! 21 pmol Ni2+ min"1 mg"1 bacterial dry weight) that functions as an energy-independent diffusion facilitator for the uptake of Ni(II) ions. This Ni2+ transport is not inhibited by similar cations such as Mn2+, Zn2+, or Co2+, but is blocked by Cu2+. Analysis of site-directed HupE mutants allowed the identification of several residues (H36, D42, H43, F69, E90, H130, and E133) that are essential for HupE-mediated Ni uptake in E. coli cells. By using translational fusions to reporter genes we demonstrated the presence of five transmembrane domains with a periplasmic N-terminal domain and a C-terminal domain buried in the lipid bilayer. The periplasmic N-terminal domain contributes to stability and functionality of the protein

More information

Item ID: 40478
DC Identifier: http://oa.upm.es/40478/
OAI Identifier: oai:oa.upm.es:40478
DOI: 10.1039/C4MT00298A
Official URL: http://pubs.rsc.org/en/content/articlelanding/2015/mt/c4mt00298a#!divAbstract
Deposited by: Memoria Investigacion
Deposited on: 13 May 2016 15:38
Last Modified: 13 May 2016 15:38
  • Logo InvestigaM (UPM)
  • Logo GEOUP4
  • Logo Open Access
  • Open Access
  • Logo Sherpa/Romeo
    Check whether the anglo-saxon journal in which you have published an article allows you to also publish it under open access.
  • Logo Dulcinea
    Check whether the spanish journal in which you have published an article allows you to also publish it under open access.
  • Logo de Recolecta
  • Logo del Observatorio I+D+i UPM
  • Logo de OpenCourseWare UPM