Open Access. Powered by Scholars. Published by Universities.®
Biochemistry, Biophysics, and Structural Biology Commons™
Open Access. Powered by Scholars. Published by Universities.®
- Discipline
- Keyword
-
- Copper (2)
- Na (2)
- ATP-binding domain (ATPBD) (1)
- ATPase transporter (1)
- Amino acids (1)
-
- Arabidopsis thaliana (1)
- Atx1 (1)
- Biochemistry (1)
- Biological Sciences (1)
- CopA (1)
- CopB (1)
- CopZ (1)
- Copper homeostasis (1)
- Crystal structure (1)
- Cu homeostasis (1)
- Cu+ (1)
- Cu+-ATPases (1)
- Cu-ATPase (1)
- Cu-transfer (1)
- ESX-3 (1)
- Efficient iron acquisition (1)
- Evolution (1)
- Gamma-proteobacteria (1)
- HITS (1)
- Homeostasis (1)
- Inner envelope (1)
- K-pump current • HeLa cells • voltage clamp • point mutation (1)
- K-pump • Na1–Na1 exchange current • HeLa cells • voltage clamp (1)
- MR-1 (1)
- Metal binding (1)
- File Type
Articles 1 - 13 of 13
Full-Text Articles in Biochemistry, Biophysics, and Structural Biology
Characterization And Structure Of A Zn2+ And [2fe-2s]-Containing Copper Chaperone From Archaeoglobus Fulgidus, Matthew Sazinsky, Benjamin Lemoine, Maria Orofino, Roman Davydov, Krisztina Bencze, Timothy Stemmler, Brian Hoffman, José Argüello, Amy Rosenzweig
Characterization And Structure Of A Zn2+ And [2fe-2s]-Containing Copper Chaperone From Archaeoglobus Fulgidus, Matthew Sazinsky, Benjamin Lemoine, Maria Orofino, Roman Davydov, Krisztina Bencze, Timothy Stemmler, Brian Hoffman, José Argüello, Amy Rosenzweig
José M. Argüello
Bacterial CopZ proteins deliver copper to P1B-type Cu+-ATPases that are homologous to the human Wilson and Menkes disease proteins. The genome of the hyperthermophile Archaeoglobus fulgidus encodes a putative CopZ copper chaperone that contains an unusual cysteine rich N-terminal domain of 130 amino acids in addition to a C-terminal copper-binding domain with a conserved CXXC motif. The N-terminal domain (CopZ-NT) is homologous to proteins found only in extremophiles and is the only such protein that is fused to a copper chaperone. Surprisingly, optical, electron paramagnetic resonance, and X-ray absorption spectroscopic data indicate the presence of a [2Fe-2S] cluster in CopZ-NT. …
A Novel Antimycobacterial Compound Acts As An Intracellular Iron Chelator., José Argüello, Marte Dragset, Glovanna Poce, Salvatore Alfonso, Teresita Padilla-Benavides, Thomas Loerger, Takushi Kaneko, James Sacchettini, Mariangela Biava, Tanya Parish, Magnus Steigedal, Eric Rubin
A Novel Antimycobacterial Compound Acts As An Intracellular Iron Chelator., José Argüello, Marte Dragset, Glovanna Poce, Salvatore Alfonso, Teresita Padilla-Benavides, Thomas Loerger, Takushi Kaneko, James Sacchettini, Mariangela Biava, Tanya Parish, Magnus Steigedal, Eric Rubin
José M. Argüello
Efficient iron acquisition is crucial for the pathogenesis of Mycobacterium tuberculosis. Mycobacterial iron uptake and metabolism are therefore attractive targets for antitubercular drug development. Resistance mutations against a novel pyrazolopyrimidinone compound (PZP) that is active against M. tuberculosis have been identified within the gene cluster encoding the ESX-3 type VII secretion system. ESX-3 is required for mycobacterial iron acquisition through the mycobactin siderophore pathway, which could indicate that PZP restricts mycobacterial growth by targeting ESX-3 and thus iron uptake. Surprisingly, we show that ESX-3 is not the cellular target of the compound. We demonstrate that PZP indeed targets iron metabolism; …
Evolution Of A Plant-Specific Copper Chaperone Family For Chloroplast Copper Homeostasis., José Argüello, Crysten Blaby-Haas, Teresita Padilla-Benavides, Roland Stube, Sabeeha Merchant
Evolution Of A Plant-Specific Copper Chaperone Family For Chloroplast Copper Homeostasis., José Argüello, Crysten Blaby-Haas, Teresita Padilla-Benavides, Roland Stube, Sabeeha Merchant
José M. Argüello
Metallochaperones traffic copper (Cu(+)) from its point of entry at the plasma membrane to its destination. In plants, one destination is the chloroplast, which houses plastocyanin, a Cu-dependent electron transfer protein involved in photosynthesis. We present a previously unidentified Cu(+) chaperone that evolved early in the plant lineage by an alternative-splicing event of the pre-mRNA encoding the chloroplast P-type ATPase in Arabidopsis 1 (PAA1). In several land plants, recent duplication events created a separate chaperone-encoding gene coincident with loss of alternative splicing. The plant-specific Cu(+) chaperone delivers Cu(+) with specificity for PAA1, which is flipped in the envelope relative to …
Periplasmic Response Upon Disruption Of Transmembrane Cu Transport In Pseudomonas Aeruginosa., José Argüello, Daniel Raimunda, Teresita Padilla-Benavides, Stefan Vogt, Sylvain Boutigny, Kaleigh Tomkinson, Lydia Finney
Periplasmic Response Upon Disruption Of Transmembrane Cu Transport In Pseudomonas Aeruginosa., José Argüello, Daniel Raimunda, Teresita Padilla-Benavides, Stefan Vogt, Sylvain Boutigny, Kaleigh Tomkinson, Lydia Finney
José M. Argüello
Pseudomonas aeruginosa, an opportunistic pathogen, has two transmembrane Cu(+) transport ATPases, CopA1 and CopA2. Both proteins export cytoplasmic Cu(+) into the periplasm and mutation of either gene leads to attenuation of virulence. CopA1 is required for maintaining cytoplasmic copper levels, while CopA2 provides copper for cytochrome c oxidase assembly. We hypothesized that transported Cu(+) ions would be directed to their destination via specific periplasmic partners and disruption of transport should affect the periplasmic copper homeostasis. Supporting this, mutation of either ATPase gene led to large increments in periplasmic cuproprotein levels. Toward identifying the proteins participating in this cellular response the …
Mechanisms Of Copper Homeostasis In Bacteria, José Argüello, Daniel Raimunda, Teresita Padilla-Benavides
Mechanisms Of Copper Homeostasis In Bacteria, José Argüello, Daniel Raimunda, Teresita Padilla-Benavides
José M. Argüello
Copper is an important micronutrient required as a redox co-factor in the catalytic centers of enzymes. However, free copper is a potential hazard because of its high chemical reactivity. Consequently, organisms exert a tight control on Cu(+) transport (entry-exit) and traffic through different compartments, ensuring the homeostasis required for cuproprotein synthesis and prevention of toxic effects. Recent studies based on biochemical, bioinformatics, and metalloproteomics approaches, reveal a highly regulated system of transcriptional regulators, soluble chaperones, membrane transporters, and target cuproproteins distributed in the various bacterial compartments. As a result, new questions have emerged regarding the diversity and apparent redundancies of …
Sinorhizobium Meliloti Nia Is A P(1b-5)-Atpase Expressed In The Nodule During Plant Symbiosis And Is Involved In Ni And Fe Transport., José Argüello, Eliza Zielazinski, Manuel Gonzalez-Guerrero, Poorna Subramanian, Timothy Stemmler, Amy Rosenzweig
Sinorhizobium Meliloti Nia Is A P(1b-5)-Atpase Expressed In The Nodule During Plant Symbiosis And Is Involved In Ni And Fe Transport., José Argüello, Eliza Zielazinski, Manuel Gonzalez-Guerrero, Poorna Subramanian, Timothy Stemmler, Amy Rosenzweig
José M. Argüello
The P1B-ATPases are a ubiquitous family of metal transporters. These transporters are classified into subfamilies on the basis of substrate specificity, which is conferred by conserved amino acids in the last three transmembrane domains. Five subfamilies have been identified to date, and representative members of four (P1B-1 to P1B-4) have been studied. The fifth family (P1B-5), of which some members contain a C-terminal hemerythrin (Hr) domain, is less well characterized. The S. meliloti Sma1163 gene encodes for a P1B-5-ATPase, denoted Nia (Nickel-iron ATPase), that is induced by exogenous Fe(2+) and Ni(2+). The nia mutant accumulates nickel and iron, suggesting a …
Conformations Of The Apo-, Substrate-Bound And Phosphate-Bound Atp-Binding Domain Of The Cu(Ii) Atpase Copb Illustrate Coupling Of Domain Movement To The Catalytic Cycle, José Argüello, Samuel Jayakanthan, Sue Roberts, Andrzej Weichsel, Megan Mcevoy
Conformations Of The Apo-, Substrate-Bound And Phosphate-Bound Atp-Binding Domain Of The Cu(Ii) Atpase Copb Illustrate Coupling Of Domain Movement To The Catalytic Cycle, José Argüello, Samuel Jayakanthan, Sue Roberts, Andrzej Weichsel, Megan Mcevoy
José M. Argüello
Heavy metal P1B-type ATPases play a critical role in cell survival by maintaining appropriate intracellular metal concentrations. Archaeoglobus fulgidus CopB is a member of this family that transports Cu(II) from the cytoplasm to the exterior of the cell using ATP as energy source. CopB has a 264 amino acid ATPBD (ATP-binding domain) that is essential for ATP binding and hydrolysis as well as ultimately transducing the energy to the transmembrane metal-binding site for metal occlusion and export. The relevant conformations of this domain during the different steps of the catalytic cycle are still under discussion. Through crystal structures of the …
Identifying Metalloproteins Through X-Ray Fluorescence Mapping And Mass Spectrometry., José Argüello, Daniel Raimunda, Tripti Khare, Carol Giometti, Stefan Vogt, Lydia Finney
Identifying Metalloproteins Through X-Ray Fluorescence Mapping And Mass Spectrometry., José Argüello, Daniel Raimunda, Tripti Khare, Carol Giometti, Stefan Vogt, Lydia Finney
José M. Argüello
Metals are critical and dynamic components of biochemistry. To understand their roles, we greatly need tools to identify the ligands that bind them within the complexity of natural systems. This work describes the development of methods that not only detect and distinguish metals, but also characterize the proteins that bind them. We describe an approach to expose, identify and quantify metalloproteins in complex mixtures by sequential non-denaturing 2D-gel electrophoresis (2D GE)/X-ray Fluorescence (XRF) and tandem mass spectrometry (MS/MS) in the same spot of a sample. We first apply the development of 2D GE/XRF to Shewanella oneidensis MR-1, a well-studied system, …
Evolution And Diversity Of Periplasmic Proteins Involved In Copper Homeostasis In Gamma Proteobacteria., José Argüello, Georgina Hernandez-Montes, Brenda Valderrama
Evolution And Diversity Of Periplasmic Proteins Involved In Copper Homeostasis In Gamma Proteobacteria., José Argüello, Georgina Hernandez-Montes, Brenda Valderrama
José M. Argüello
Background: Different systems contributing to copper homeostasis in bacteria have been described in recent years involving periplasmic and transport proteins that provide resistance via metal efflux to the extracellular media (CopA/Cue, Cus, Cut, and Pco). The participation of these proteins in the assembly of membrane, periplasmic and secreted cuproproteins has also been postulated. The integration and interrelation of these systems and their apparent redundancies are less clear since they have been studied in alternative systems. Based on the idea that cellular copper is not free but rather it is transferred via protein-protein interactions, we hypothesized that systems would coevolve and …
A Novel Zinc Binding System, Zevab, Is Critical For Survival Of Nontypeable Haemophilus Influenzae In A Murine Lung Infection Model., José Argüello, Charles Rosadini, Jeffery Gawronski, Daniel Raimunda, Brian Akerley
A Novel Zinc Binding System, Zevab, Is Critical For Survival Of Nontypeable Haemophilus Influenzae In A Murine Lung Infection Model., José Argüello, Charles Rosadini, Jeffery Gawronski, Daniel Raimunda, Brian Akerley
José M. Argüello
Nontypeable Haemophilus influenzae (NTHI) is a Gram-negative bacterial pathogen that causes upper and lower respiratory infections. Factors required for pulmonary infection by NTHI are not well understood. Previously, using high-throughput insertion tracking by deep sequencing (HITS), putative lung colonization factors were identified. Also, previous research indicates that secreted disulfide-dependent factors are important for virulence of H. influenzae. In the present study, HITS data were compared with an informatics-based list of putative substrates of the periplasmic oxidoreductase DsbA to find and characterize secreted virulence factors. This analysis resulted in identification of the "zinc binding essential for virulence" (zev) locus consisting of …
Mechanism Of Cu+-Transporting Atpases: Soluble Cu+ Chaperones Directly Transfer Cu+ To Transmembrane Transport Sites, José Argüello, Manuel Gonzalez-Guerrero
Mechanism Of Cu+-Transporting Atpases: Soluble Cu+ Chaperones Directly Transfer Cu+ To Transmembrane Transport Sites, José Argüello, Manuel Gonzalez-Guerrero
José M. Argüello
As in other P-type ATPases, metal binding to transmembrane metal-binding sites (TM-MBS) in Cu(+)-ATPases is required for enzyme phosphorylation and subsequent transport. However, Cu(+) does not access Cu(+)-ATPases in a free (hydrated) form but is bound to a chaperone protein. Cu(+) transfer from Cu(+) chaperones to regulatory cytoplasmic metal-binding domains (MBDs) present in these ATPases has been described, but there is no evidence of a proposed subsequent Cu(+) movement from the MBDs to the TM-MBS. Alternatively, we postulate the parsimonious Cu(+) transfer by the chaperone directly to TM-MBS. Testing both models, the delivery of Cu(+) by Archaeoglobus fulgidus Cu(+) chaperone …
Electrogenic Sodium–Sodium Exchange Carried Out By Na,K-Atpase Containing The Amino Acid Substitution Glu779ala, José Argüello, R.Daniel Peluffo, Jerry Lingrel, Joshua Berlin
Electrogenic Sodium–Sodium Exchange Carried Out By Na,K-Atpase Containing The Amino Acid Substitution Glu779ala, José Argüello, R.Daniel Peluffo, Jerry Lingrel, Joshua Berlin
José M. Argüello
Na,K-ATPase containing the amino acid substitution glutamate to alanine at position 779 of the a subunit (Glu779Ala) supports a high level of Na-ATPase and electrogenic Na1–Na1 exchange activityin the absence of K1. In microsomal preparations of Glu779Ala enzyme, the Na1 concentration for half maximal activation of Na-ATPase activity was 161 6 14 mM (n 5 3). Furthermore, enzyme activity with 800 mM Na1 was found to be similar in the presence and absence of 20 mM K1. These results showed that Na1, with low affinity, could stimulate enzyme turnover as effectively as K1. To gain further insight into the mechanism …
The Role Of Na,K-Atpase Alpha Subunit Serine 775 And Glutamate 779 In Determining The Extracellular K+ And Membrane Potential-Dependent Properties Of The Na,K-Pump, José Argüello, R.Daniel Peluffo, Joshua Berlin
The Role Of Na,K-Atpase Alpha Subunit Serine 775 And Glutamate 779 In Determining The Extracellular K+ And Membrane Potential-Dependent Properties Of The Na,K-Pump, José Argüello, R.Daniel Peluffo, Joshua Berlin
José M. Argüello
The roles of Ser775 and Glu779, two amino acids in the putative fifth transmembrane segment of the Na,K-ATPase a subunit, in determining the voltage and extracellular K1 (K1o) dependence of enzyme-mediated ion transport, were examined in this study. HeLa cells expressing the a1 subunit of sheep Na,K-ATPase were voltage clamped via patch electrodes containing solutions with 115 mM Na1 (378C). Na,K-pump current produced by the ouabain-resistant control enzyme (RD), containing amino acid substitutions Gln111Arg and Asn122Asp, displayed a membrane potential and K1o dependence similar to wild-type Na,K-ATPase during superfusion with 0 and 148 mM Na1-containing salt solutions. Additional substitution of …