Rhizobium leguminosarum HupE is a highly-specific diffusion facilitator for nickel uptake
| Autor: | Agnès Rodrigue, Belén Brito, Marta Albareda, José Manuel Palacios, Tomás Ruiz-Argüeso, Marie Andrée Mandrand-Berthelot, Juan Imperial |
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| Přispěvatelé: | Universidad Politécnica de Madrid (UPM), Microbiologie, adaptation et pathogénie (MAP), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS), Trafic et signalisation membranaires chez les bactéries (MTSB), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Institut National des Sciences Appliquées (INSA)-Université de Lyon-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS), Institut National des Sciences Appliquées (INSA)-Université de Lyon-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL) |
| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
inorganic chemicals
Hydrogenase Stereochemistry Lipid Bilayers Molecular Sequence Data Biophysics chemistry.chemical_element Biology medicine.disease_cause Ligands Biochemistry Rhizobium leguminosarum Biomaterials 03 medical and health sciences Bacterial Proteins Genes Reporter Nickel [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN] medicine Escherichia coli Amino Acid Sequence Lipid bilayer 030304 developmental biology 0303 health sciences 030306 microbiology Permease Agricultura Metals and Alloys Membrane Proteins [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biology Periplasmic space [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology Protein Structure Tertiary [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM] Transmembrane domain chemistry Chemistry (miscellaneous) Mutation Mutagenesis Site-Directed |
| Zdroj: | Metallomics Metallomics, Royal Society of Chemistry, 2015, 7 (4), pp.691-701. ⟨10.1039/c4mt00298a⟩ Metallomics, ISSN 1756-5901, 2015, Vol. 7 Archivo Digital UPM Universidad Politécnica de Madrid |
| ISSN: | 1756-5901 1756-591X |
| DOI: | 10.1039/c4mt00298a⟩ |
| Popis: | International audience; 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 K m 227 AE 21 nM; V max 49 AE 21 pmol Ni 2+ min À1 mg À1 bacterial dry weight) that functions as an energy-independent diffusion facilitator for the uptake of Ni(II) ions. This Ni 2+ transport is not inhibited by similar cations such as Mn 2+ , Zn 2+ , or Co 2+ , but is blocked by Cu 2+. 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. |
| Databáze: | OpenAIRE |
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