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Full-Text Articles in Biochemistry, Biophysics, and Structural Biology
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 …