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Copper chaperone

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https://www.readbyqxmd.com/read/28780408/an-essential-role-of-n-terminal-domain-of-copper-chaperone-in-the-enzymatic-activation-of-cu-zn-superoxide-dismutase
#1
Mami Fukuoka, Eiichi Tokuda, Kenta Nakagome, Zhiliang Wu, Isao Nagano, Yoshiaki Furukawa
Cu/Zn-superoxide dismutase (SOD1) is an enzyme that disproportionates superoxide anion into hydrogen peroxide and molecular oxygen. The enzymatic activity of SOD1 requires the binding of copper and zinc ions and also the formation of a conserved intramolecular disulfide bond. In a eukaryotic cell, a copper chaperone for SOD1 (CCS) has been known to supply a copper ion and also introduce the disulfide bond into SOD1; however, a mechanism controlling the CCS-dependent activation of SOD1 remains obscure. Here, we characterized CCS isolated from a human liver fluke, Clonorchis sinensis, and found that an N-terminal domain of CCS was essential in supplying a copper ion in SOD1...
July 31, 2017: Journal of Inorganic Biochemistry
https://www.readbyqxmd.com/read/28760827/copper-homeostasis-networks-in-the-bacterium-pseudomonas-aeruginosa
#2
Julia Quintana, Lorena Novoa-Aponte, José M Argüello
Bacterial copper (Cu(+)) homeostasis enables both precise metallation of diverse cuproproteins and control of variable metal levels. To this end, protein networks mobilize Cu(+) to cellular targets with remarkable specificity. However, the understanding of these processes is rather fragmented. Here, we use genome-wide transcriptomic analysis by RNA-Seq to characterize the response of Pseudomonas aeruginosa to external 0.5 mM CuSO4, a condition that did not generate pleiotropic effects. Pre-steady (5 min) and steady state (2 h) Cu(+) fluxes, resulted in distinct transcriptome landscapes...
July 31, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28711491/copper-chaperone-atox1-regulates-pluripotency-factor-oct4-in-preimplantation-mouse-embryos
#3
Emanuele Celauro, Amisa Mukaj, Juan Carlos Fierro-González, Pernilla Wittung-Stafshede
Despite of the importance of copper (Cu) during pregnancy, the roles of Cu-binding proteins during early embryonic development are unknown. The Cu chaperone ATOX1 was recently suggested to have additional functions related to transcription and cancer. When we analyzed single-cell RNA transcript data from early mouse embryos, Atox1 transcript levels increased dramatically at the 8-cell stage and, at 16- and 32-cell embryo stages, matched those of Oct4 which expresses a transcription factor essential for pluripotency in the inner cell mass...
July 12, 2017: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/28689066/roles-of-a-mitochondrial-accsco2-gene-from-apis-cerana-cerana-in-oxidative-stress-responses
#4
Haihong Jia, Manli Ma, Na Zhai, Zhenguo Liu, Hongfang Wang, Xingqi Guo, Baohua Xu
In eukaryotes, cytochrome c oxidase (COX) is a multimeric protein complex that is the last enzyme in the respiratory electron transport chain of mitochondria. Syntheses of cytochrome c oxidase (SCO) proteins are copper-donor chaperones involved in metalation of the CuA redox center of COX. However, its other precise actions are not yet understood. Here, we report the characterization of AccSCO2 from Apis cerana cerana (Acc). Our data showed that AccSCO2 expression was induced by cold (4°C), CdCl2, HgCl2, ultraviolet (UV) light, and H2O2 and was inhibited by different pesticide treatments...
July 2, 2017: Journal of Inorganic Biochemistry
https://www.readbyqxmd.com/read/28686251/oxygen-dependent-activation-of-cu-zn-superoxide-dismutase-1
#5
REVIEW
Morgan M Fetherolf, Stefanie D Boyd, Duane D Winkler, Dennis R Winge
Copper zinc superoxide dismutase (Sod1) is a critical enzyme in limiting reactive oxygen species in both the cytosol and the mitochondrial intermembrane space. Sod1 dismutes superoxide anions to hydrogen peroxide and oxygen. The catalytic reaction is dependent on an active site copper ion and a disulfide bonded conformation. The activation of Sod1 is mediated by its chaperone Ccs1. The mechanism of Ccs1-mediated Sod1 activation involves both insertion of the catalytic copper ion and mediating disulfide bond formation...
August 16, 2017: Metallomics: Integrated Biometal Science
https://www.readbyqxmd.com/read/28685789/orchestration-of-dynamic-copper-navigation-new-and-missing-pieces
#6
REVIEW
Helena Öhrvik, Jan Aaseth, Nina Horn
A general principle in all cells in the body is that an essential metal - here copper - is taken up at the plasma membrane, directed through cellular compartments for use in specific enzymes and pathways, stored in specific scavenging molecules if in surplus, and finally expelled from the cells. Here we attempt to provide a critical view on key concepts involved in copper transfer across membranes and through compartments in the human body. The focus of this review is on the influence of bioinorganic and thermodynamic rules on the flow in cellular copper networks...
July 7, 2017: Metallomics: Integrated Biometal Science
https://www.readbyqxmd.com/read/28653724/probing-functional-roles-of-wilson-disease-protein-atp7b-copper-binding-domains-in-yeast
#7
Kumaravel Ponnandai Shanmugavel, Dina Petranovic, Pernilla Wittung-Stafshede
After Ctr1-mediated uptake into human cells, copper (Cu) ions are transported by the cytoplasmic Cu chaperone Atox1 to the Wilson disease protein (ATP7B) in the Golgi network. Cu transfer occurs via direct protein-protein interactions and leads to incorporation of Cu into Cu-dependent enzymes. ATP7B is a large multi-domain membrane-spanning protein which, in contrast to homologs, has six cytoplasmic metal-binding domains (MBDs). The reason for multiple MBDs is proposed to be indirect modulation of activity but mechanistic studies of full-length ATP7B are limited...
July 19, 2017: Metallomics: Integrated Biometal Science
https://www.readbyqxmd.com/read/28549213/binding-of-copper-and-cisplatin-to-atox1-is-mediated-by-glutathione-through-the-formation-of-metal-sulfur-clusters
#8
Natalia V Dolgova, Corey Yu, John P Cvitkovic, Miroslav Hodak, Kurt H Nienaber, Kelly L Summers, Julien J H Cotelesage, Jerzy Bernholc, George A Kaminski, Ingrid J Pickering, Graham N George, Oleg Y Dmitriev
Copper is an essential nutrient required for many biological processes involved in primary metabolism, but free copper is toxic due to its ability to catalyze formation of free radicals. To prevent toxic effects, in the cell copper is bound to proteins and low molecular weight compounds, such as glutathione, at all times. The widely used chemotherapy agent cisplatin is known to bind to copper-transporting proteins, including copper chaperone Atox1. Cisplatin interactions with Atox1 and other copper transporters are linked to cancer resistance to platinum-based chemotherapy...
June 9, 2017: Biochemistry
https://www.readbyqxmd.com/read/28543811/the-structural-flexibility-of-the-human-copper-chaperone-atox1-insights-from-combined-pulsed-epr-studies-and-computations
#9
Ariel R Levy, Meital Turgeman, Lada Gevorkyan-Aiapetov, Sharon Ruthstein
Metallochaperones are responsible for shuttling metal ions to target proteins. Thus, a metallochaperone's structure must be sufficiently flexible both to hold onto its ion while traversing the cytoplasm and to transfer the ion to or from a partner protein. Here, we sought to shed light on the structure of Atox1, a metallochaperone involved in the human copper regulation system. Atox1 shuttles copper ions from the main copper transporter, Ctr1, to the ATP7b transporter in the Golgi apparatus. Conventional biophysical tools such as X-ray or NMR cannot always target the various conformational states of metallochaperones, owing to a requirement for crystallography or low sensitivity and resolution...
August 2017: Protein Science: a Publication of the Protein Society
https://www.readbyqxmd.com/read/28533431/copper-zinc-superoxide-dismutase-is-activated-through-a-sulfenic-acid-intermediate-at-a-copper-ion-entry-site
#10
Morgan M Fetherolf, Stefanie D Boyd, Alexander B Taylor, Hee Jong Kim, James A Wohlschlegel, Ninian J Blackburn, P John Hart, Dennis R Winge, Duane D Winkler
Metallochaperones are a diverse family of trafficking molecules that provide metal ions to protein targets for use as cofactors. The copper chaperone for superoxide dismutase (Ccs1) activates immature copper-zinc superoxide dismutase (Sod1) by delivering copper and facilitating the oxidation of the Sod1 intramolecular disulfide bond. Here, we present structural, spectroscopic, and cell-based data supporting a novel copper-induced mechanism for Sod1 activation. Ccs1 binding exposes an electropositive cavity and proposed "entry site" for copper ion delivery on immature Sod1...
July 21, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28466911/stepwise-copper-i-binding-to-metallothionein-a-mixed-cooperative-and-non-cooperative-mechanism-for-all-20-copper-ions
#11
Judith S Scheller, Gordon W Irvine, Daisy L Wong, Andrea Hartwig, Martin J Stillman
Copper is a ubiquitous trace metal of vital importance in that it serves as a cofactor in many metalloenzymes. Excess copper becomes harmful if not sequestered appropriately in the cell. As a metal ion chaperone, metallothionein (MT) has been proposed as a key player in zinc and copper homeostasis within the cell. The underlying mechanisms by which MT sequesters and transfers copper ions, and subsequently achieves its proposed biological function remain unknown. Using a combination of electrospray ionization mass spectrometry (ESI-MS), circular dichroism (CD), and emission spectroscopy, we report that the Cu(i) to human apo-MT1a binding mechanism is highly pH-dependent...
May 24, 2017: Metallomics: Integrated Biometal Science
https://www.readbyqxmd.com/read/28433108/genetic-and-environmental-modifiers-of-wilson-disease
#12
Valentina Medici, Karl-Heinz Weiss
Wilson disease (WD) is characterized by remarkable variety in its phenotypic presentation. Patients with WD can present with hepatic, neurologic, and psychiatric symptoms combined in different and unpredictable ways. Importantly, no convincing phenotype-genotype correlation has ever been identified, opening the possibility that other genes, aside from ATPase copper-transporting beta (ATP7B), are involved in the pathogenesis of this condition. In addition, modifier genes, or genes that can affect the expression of other genes, may be involved...
2017: Handbook of Clinical Neurology
https://www.readbyqxmd.com/read/28428045/sco2-deficient-mice-develop-increased-adiposity-and-insulin-resistance
#13
Shauna Hill, Sathyaseelan S Deepa, Kavithalakshmi Sataranatarajan, Pavithra Premkumar, Daniel Pulliam, Yuhong Liu, Vanessa Y Soto, Kathleen E Fischer, Holly Van Remmen
Cytochrome c oxidase (COX) is an essential transmembrane protein complex (Complex IV) in the mitochondrial respiratory electron chain. Mutations in genes responsible for the assembly of COX are associated with Leigh syndrome, cardiomyopathy, spinal muscular atrophy and other fatal metabolic disorders in humans. Previous studies have shown that mice lacking the COX assembly protein Surf1 (Surf1(-/-) mice) paradoxically show a number of beneficial metabolic phenotypes including increased insulin sensitivity, upregulation of mitochondrial biogenesis, induction of stress response pathways and increased lifespan...
April 18, 2017: Molecular and Cellular Endocrinology
https://www.readbyqxmd.com/read/28294521/thiol-based-copper-handling-by-the-copper-chaperone-atox1
#14
REVIEW
Yuta Hatori, Sachiye Inouye, Reiko Akagi
Human antioxidant protein 1 (Atox1) plays a crucial role in cellular copper homeostasis. Atox1 captures cytosolic copper for subsequent transfer to copper pumps in trans Golgi network, thereby facilitating copper supply to various copper-dependent oxidereductases matured within the secretory vesicles. Atox1 and other copper chaperones handle cytosolic copper using Cys thiols which are ideal ligands for coordinating Cu(I). Recent studies demonstrated reversible oxidation of these Cys residues in copper chaperones, linking cellular redox state to copper homeostasis...
March 15, 2017: IUBMB Life
https://www.readbyqxmd.com/read/28217917/a-comprehensive-phylogenetic-analysis-of-copper-transporting-p1b-atpases-from-bacteria-of-the-rhizobiales-order-uncovers-multiplicity-diversity-and-novel-taxonomic-subtypes
#15
Ciro Cubillas, Fabiola Miranda-Sánchez, Antonio González-Sánchez, José Pedro Elizalde, Pablo Vinuesa, Susana Brom, Alejandro García-de Los Santos
The ubiquitous cytoplasmic membrane copper transporting P1B-1 and P1B-3 -type ATPases pump out Cu(+) and Cu(2+) , respectively, to prevent cytoplasmic accumulation and avoid toxicity. The presence of five copies of Cu-ATPases in the symbiotic nitrogen-fixing bacteria Sinorhizobium meliloti is remarkable; it is the largest number of Cu(+) -transporters in a bacterial genome reported to date. Since the prevalence of multiple Cu-ATPases in members of the Rhizobiales order is unknown, we performed an in silico analysis to understand the occurrence, diversity and evolution of Cu(+) -ATPases in members of the Rhizobiales order...
August 2017: MicrobiologyOpen
https://www.readbyqxmd.com/read/28212901/the-dissociation-of-the-hsp60-pro-caspase-3-complex-by-bis-pyridyl-oxadiazole-copper-complex-cubipyoxa-leads-to-cell-death-in-nci-h292-cancer-cells
#16
Celeste Caruso Bavisotto, Dragana Nikolic, Antonella Marino Gammazza, Rosario Barone, Filippa Lo Cascio, Emanuele Mocciaro, Giovanni Zummo, Everly Conway de Macario, Alberto Jl Macario, Francesco Cappello, Valentina Giacalone, Andrea Pace, Giampaolo Barone, Antonio Palumbo Piccionello, Claudia Campanella
Cell survival and proliferation are central to carcinogenesis, involving various mechanisms among which those that impede apoptosis are important. In this, the role of the molecular chaperone Hsp60 is unclear since it has been reported that it can be both, pro- or anti-apoptotic. A solution to this riddle is crucial to the development of anti-cancer therapies targeting Hsp60. We addressed this question using a tumor cell line, NCI-H292, and [Cu(3,5-bis(2'-pyridyl)-1,2,4-oxadiazole)2(H2O)2](ClO4)2, CubipyOXA, a copper-containing compound with cytotoxic properties...
May 2017: Journal of Inorganic Biochemistry
https://www.readbyqxmd.com/read/28120938/s-acylation-of-sod1-ccs-and-a-stable-sod1-ccs-heterodimer-in-human-spinal-cords-from-als-and-non-als-subjects
#17
Sarah E Antinone, Ghanashyam D Ghadge, Lyle W Ostrow, Raymond P Roos, William N Green
Previously, we found that human Cu, Zn-superoxide dismutase (SOD1) is S-acylated (palmitoylated) in vitro and in amyotrophic lateral sclerosis (ALS) mouse models, and that S-acylation increased for ALS-causing SOD1 mutants relative to wild type. Here, we use the acyl resin-assisted capture (acyl-RAC) assay to demonstrate S-acylation of SOD1 in human post-mortem spinal cord homogenates from ALS and non-ALS subjects. Acyl-RAC further revealed that endogenous copper chaperone for SOD1 (CCS) is S-acylated in both human and mouse spinal cords, and in vitro in HEK293 cells...
January 25, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28107647/programmed-ribosomal-frameshifting-generates-a-copper-transporter-and-a-copper-chaperone-from-the-same-gene
#18
Sezen Meydan, Dorota Klepacki, Subbulakshmi Karthikeyan, Tõnu Margus, Paul Thomas, John E Jones, Yousuf Khan, Joseph Briggs, Jonathan D Dinman, Nora Vázquez-Laslop, Alexander S Mankin
Metal efflux pumps maintain ion homeostasis in the cell. The functions of the transporters are often supported by chaperone proteins, which scavenge the metal ions from the cytoplasm. Although the copper ion transporter CopA has been known in Escherichia coli, no gene for its chaperone had been identified. We show that the CopA chaperone is expressed in E. coli from the same gene that encodes the transporter. Some ribosomes translating copA undergo programmed frameshifting, terminate translation in the -1 frame, and generate the 70 aa-long polypeptide CopA(Z), which helps cells survive toxic copper concentrations...
January 19, 2017: Molecular Cell
https://www.readbyqxmd.com/read/28107645/a-cu-rious-ribosomal-profiling-pattern-leads-to-the-discovery-of-ribosomal-frameshifting-in-the-synthesis-of-a-copper-chaperone
#19
John F Atkins, Gary Loughran, Pavel V Baranov
In many bacteria, separate genes encode a copper binding chaperone and a copper efflux pump, but in some the chaperone encoding gene has been elusive. In this issue of Molecular Cell, Meydan et al. (2017) report that ribosomes translating the ORF that encodes the copper pump frequently frameshift and terminate to produce the copper chaperone.
January 19, 2017: Molecular Cell
https://www.readbyqxmd.com/read/28078344/kinetic-analysis-of-copper-transfer-from-a-chaperone-to-its-target-protein-mediated-by-complex-formation
#20
Kristine L Kay, Liang Zhou, Leonardo Tenori, Justin M Bradley, Chloe Singleton, Margaret A Kihlken, Simone Ciofi-Baffoni, Nick E Le Brun
Chaperone proteins that traffic copper around the cell minimise its toxicity by maintaining it in a tightly bound form. The transfer of copper from chaperones to target proteins is promoted by complex formation, but the kinetic characteristics of transfer have yet to be demonstrated for any chaperone-target protein pair. Here we report studies of copper transfer between the Atx1-type chaperone CopZ from Bacillus subtilis and the soluble domains of its cognate P-type ATPase transporter, CopAab. Transfer of copper from CopZ to CopAab was found to occur rapidly, with a rate constant at 25 °C of ∼267 s(-1), many orders of magnitude higher than that for Cu(i) dissociation from CopZ in the absence of CopAab...
January 12, 2017: Chemical Communications: Chem Comm
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