Metal-Binding Thermodynamics of the Histidine-Rich Sequence from the Metal-Transport Protein IRT1 ofArabidopsisthaliana

2006 ◽  
Vol 45 (21) ◽  
pp. 8500-8508 ◽  
Author(s):  
Nicholas E. Grossoehme ◽  
Shreeram Akilesh ◽  
Mary Lou Guerinot ◽  
Dean E. Wilcox
Keyword(s):  
Metal Binding ◽  
Metal Transport ◽  
Transport Protein ◽  
Binding Thermodynamics

scholarly journals Metal-Binding Thermodynamics of the Histidine-Rich Sequence from the Metal-Transport Protein IRT1 ofArabidopsis thaliana.

2006 ◽  
Vol 45 (21) ◽  
pp. 8812-8812 ◽  
Author(s):  
Nicholas E. Grossoehme ◽  
Shreeram Akilesh ◽  
Mary Lou Guerinot ◽  
Dean E. Wilcox
Keyword(s):  
Metal Binding ◽  
Metal Transport ◽  
Transport Protein ◽  
Binding Thermodynamics ◽  
Ofarabidopsis Thaliana

scholarly journals Transcriptional activation and localization of expression of Brassica juncea putative metal transport protein BjMTP1

2007 ◽  
Vol 7 (1) ◽  
pp. 32 ◽  
Author(s):  
Balasubramaniam Muthukumar ◽  
Bakhtiyor Yakubov ◽  
David E Salt
Keyword(s):  
Brassica Juncea ◽  
Transcriptional Activation ◽  
Metal Transport ◽  
Transport Protein

Nickel-responsive transcriptional regulators

Metallomics ◽  
2015 ◽  
Vol 7 (9) ◽  
pp. 1305-1318 ◽  
Author(s):  
Francesco Musiani ◽  
Barbara Zambelli ◽  
Micaela Bazzani ◽  
Luca Mazzei ◽  
Stefano Ciurli
Keyword(s):  
Metal Binding ◽  
Transcriptional Regulators ◽  
Structural Features ◽  
Metal Coordination ◽  
Coordination Modes ◽  
Binding Thermodynamics

The structural features, metal coordination modes and metal binding thermodynamics of known Ni(ii)-dependent transcriptional regulators are highlighted and discussed.

Cell-wall-bound metal ions are not taken up inNeurospora crassa

2005 ◽  
Vol 51 (12) ◽  
pp. 1021-1026 ◽  
Author(s):  
J Naveena Lavanya Latha ◽  
K Rashmi ◽  
P Maruthi Mohan
Keyword(s):  
Cell Wall ◽  
Neurospora Crassa ◽  
Metal Binding ◽  
Metal Ion ◽  
Resistant Mutant ◽  
Metal Transport ◽  
Cobalt Uptake ◽  
Magnesium Surface ◽  
Dose Dependent ◽  
Binding Cell

To establish the relevance of the cell wall in metal ion transport, cobalt uptake was examined in Neurospora crassa. Cobalt taken up was largely surface bound (>90%), resulting in a release of calcium and magnesium. Surface-bound cobalt could not enter intracellular locations upon further incubation of mycelia in a metal-free medium. Saturation of the surface with one metal augured subsequent dose-dependent entry of a different metal into intracellular locations. In comparison with the cobalt-resistant mutant, the cobalt-sensitive strain of N. crassa bound less cobalt on the surface but with significant intracellular accumulation. Our results demonstrate the importance of the cell wall in metal transport, toxicity, and resistance in fungi.Key words: metal transport, metal binding, cell wall, biosorption, Neurospora crassa.

The N-terminal degenerated metal-binding domain is involved in the heavy metal transport activity of TaHMA2

2015 ◽  
Vol 34 (9) ◽  
pp. 1615-1628 ◽  
Author(s):  
Shuqin Xiang ◽  
Shanshan Feng ◽  
Yuxiu Zhang ◽  
Jinjuan Tan ◽  
Shuang Liang ◽  
...  
Keyword(s):  
Heavy Metal ◽  
Metal Binding ◽  
Metal Transport ◽  
Binding Domain ◽  
Transport Activity ◽  
Metal Binding Domain ◽  
Heavy Metal Transport

scholarly journals Transcriptional Regulation, Metal Binding Properties and Structure of Pden1597, an Unusual Zinc Transport Protein fromParacoccus denitrificans

2015 ◽  
Vol 290 (19) ◽  
pp. 11878-11889 ◽  
Author(s):  
Melody Handali ◽  
Durga P. Neupane ◽  
Hridindu Roychowdhury ◽  
Erik T. Yukl
Keyword(s):  
Transcriptional Regulation ◽  
Metal Binding ◽  
Transport Protein ◽  
Zinc Transport ◽  
Binding Properties

scholarly journals Transmembrane helix 6b links proton- and metal-release pathways to drive conformational change in an Nramp transition metal transporter

2019 ◽  
Author(s):  
Aaron T. Bozzi ◽  
Anne L. McCabe ◽  
Benjamin C. Barnett ◽  
Rachelle Gaudet
Keyword(s):  
Transition Metal ◽  
Conformational Change ◽  
Metal Binding ◽  
Deinococcus Radiodurans ◽  
Transmembrane Helix ◽  
Metal Transport ◽  
Natural Resistance ◽  
Metal Release ◽  
Transport Pathway ◽  
Exit Route

ABSTRACTThe natural resistance-associated macrophage protein (Nramp) family encompasses transition metal and proton co-transporters found in organisms from bacteria to humans. Recent structures ofDeinococcus radiodurans(Dra)Nramp in multiple conformations revealed the intramolecular rearrangements required for alternating access. Here we demonstrate that two parallel cytoplasm-accessible networks of conserved hydrophilic residues in DraNramp—one lining the wide intracellular vestibule for metal release, the other forming a narrow proton-transport pathway—are essential for metal transport. We further show that mutagenic or post-translational modifications of transmembrane helix (TM) 6b, which structurally links these two pathways, impedes normal conformational cycling and metal transport. TM6b contains two highly conserved histidines, H232 and H237. Different mutagenic perturbations for H232, just below the metal-binding site along the proton-exit route, differentially affect DraNramp’s conformational state, suggesting H232 serves as a pivot point for conformational change. In contrast, any tested replacement for H237, lining the metal-exit route, locks the transporter in a transport-inactive outward-closed state. We conclude that these two histidines, and TM6b more broadly, help trigger the bulk rearrangement to the inward-open state upon metal binding and facilitate the return of the empty transporter to an outward-open state upon metal release.

scholarly journals Proton co-transport and voltage dependence enforce unidirectional metal transport in an Nramp transporter

2018 ◽  
Author(s):  
Aaron T. Bozzi ◽  
Lukas B. Bane ◽  
Christina M. Zimanyi ◽  
Rachelle Gaudet
Keyword(s):  
Metal Binding ◽  
Voltage Dependence ◽  
Mechanistic Model ◽  
Salt Bridge ◽  
Metal Transport ◽  
Natural Resistance ◽  
Metal Type ◽  
Proton Symport ◽  
Macrophage Protein ◽  
Stimulation Of

AbstractSecondary transporters harness electrochemical energy to move substrate through structurally-enforced co-substrate “coupling”. We untangle the “proton-metal coupling” behavior by a Natural resistance-associated macrophage protein (Nramp) transporter into two distinct phenomena: ΔpH stimulation of metal transport and metal stimulation of proton co-transport. Surprisingly, metal type dictates co-transport stoichiometry, leading to manganese-proton symport but cadmium uniport. Additionally, the membrane potential affects both the kinetics and thermodynamics of metal transport. A conserved salt-bridge network near the metal-binding site imparts voltage dependence and enables proton co-transport, properties that allow this Nramp transporter to maximize metal uptake and prevent deleterious back-transport of acquired metals. We provide a new mechanistic model for Nramp metal-proton symport in which, in addition to substrate gradients determining directionality as in canonical secondary transport, synergy between protein structure and physiological voltage enforces unidirectional substrate movement. Our results illustrate a functional advantage that arises from deviations from the traditional model of symport.

Selective Binding of Trivalent Metals by Hexahomotrioxacalix[3]arene Macrocycles:  Determination of Metal-Binding Constants and Metal Transport Studies

1997 ◽  
Vol 36 (14) ◽  
pp. 2956-2959 ◽  
Author(s):  
Philip D. Hampton ◽  
Charles E. Daitch ◽  
Amy M. Shachter
Keyword(s):  
Metal Binding ◽  
Binding Constants ◽  
Metal Transport ◽  
Selective Binding ◽  
Transport Studies ◽  
Trivalent Metals

scholarly journals Cucumber metal transport protein MTP8 confers increased tolerance to manganese when expressed in yeast and Arabidopsis thaliana

2014 ◽  
Vol 65 (18) ◽  
pp. 5367-5384 ◽  
Author(s):  
Magdalena Migocka ◽  
Anna Papierniak ◽  
Ewa Maciaszczyk-Dziubińska ◽  
Piotr Poździk ◽  
Ewelina Posyniak ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Metal Transport ◽  
Transport Protein
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