scholarly journals A cytosolic copper storage protein provides a second level of copper tolerance inStreptomyces lividans

Metallomics ◽  
2018 ◽  
Vol 10 (1) ◽  
pp. 180-193 ◽  
Author(s):  
Megan L. Straw ◽  
Amanda K. Chaplin ◽  
Michael A. Hough ◽  
Jordi Paps ◽  
Vassiliy N. Bavro ◽  
...  
Keyword(s):  
Storage Protein ◽  
Streptomyces Lividans ◽  
Copper Resistance ◽  
Copper Tolerance ◽  
Copper Storage

A cytosolic copper storage protein has been identified inStreptomyces lividansand plays a role in copper tolerance once the first layer of copper resistance becomes saturated.

scholarly journals Redesign of a Copper Storage Protein into an Artificial Hydrogenase

ACS Catalysis ◽  
2019 ◽  
Vol 9 (7) ◽  
pp. 5847-5859 ◽  
Author(s):  
Dhanashree Selvan ◽  
Pallavi Prasad ◽  
Erik R. Farquhar ◽  
Yelu Shi ◽  
Skyler Crane ◽  
...  
Keyword(s):  
Storage Protein ◽  
Copper Storage

Occurrence of cop-like copper resistance genes among bacteria isolated from a water distribution system

1995 ◽  
Vol 41 (7) ◽  
pp. 642-646 ◽  
Author(s):  
Chuzhao Lin ◽  
Betty H. Olson
Keyword(s):  
Pseudomonas Syringae ◽  
Resistance Genes ◽  
Distribution System ◽  
Water Distribution ◽  
Water Distribution System ◽  
Culture Media ◽  
Copper Resistance ◽  
Copper Tolerance ◽  
Resistant Bacteria ◽  
Copper Resistance Genes

The occurrence of cop-like copper resistance determinants homologous to the cop genes of Pseudomonas syringae among bacteria isolated from a water distribution system experiencing copper corrosion was investigated in this study. It was found that at least 49% of the copper-resistant bacteria and less than 15% of the copper-sensitive isolates possessed a cop homolog. The occurrence of this determinant in the copper-resistant population correlated with the degree of copper tolerance exhibited by the bacteria. The effect of organic substances present in the culture media on the empirical degree of bacterial copper tolerance is also discussed.Key words: copper resistance genes, water distribution system, cop.

scholarly journals The oxygen reactivity of an artificial hydrogenase designed in a reengineered copper storage protein

2020 ◽  
Vol 49 (6) ◽  
pp. 1928-1934
Author(s):  
Dhanashree Selvan ◽  
Yelu Shi ◽  
Pallavi Prasad ◽  
Skyler Crane ◽  
Yong Zhang ◽  
...  
Keyword(s):  
Storage Protein ◽  
Binding Protein ◽  
Nickel Binding ◽  
Copper Storage ◽  
Oxygen Reactivity

The O2 reactivity of an artificial biomolecular hydrogenase, the nickel binding protein (NBP) is investigated.

scholarly journals Comparative Genomic Analysis of Bacillus thuringiensis Reveals Molecular Adaptations to Copper Tolerance

2018 ◽  
Author(s):  
Low Yi Yik ◽  
Grace Joy Wei Lie Chin ◽  
Collin Glen Joseph ◽  
Kenneth Francis Rodrigues
Keyword(s):  
Bacillus Thuringiensis ◽  
Extreme Environments ◽  
Genomic Analysis ◽  
Comparative Genomic Analysis ◽  
Copper Resistance ◽  
Copper Tolerance ◽  
Contaminated Site ◽  
Comparative Genomic ◽  
Wide Range ◽  
Almost All

ABSTRACTBacillus thuringiensis is a type of Gram positive and rod shaped bacterium that is found in a wide range of habitats. Despite the intensive studies conducted on this bacterium, most of the information available are related to its pathogenic characteristics, with only a limited number of publications mentioning its ability to survive in extreme environments. Recently, a B. thuringiensis MCMY1 strain was successfully isolated from a copper contaminated site in Mamut Copper Mine, Sabah. This study aimed to conduct a comparative genomic analysis by using the genome sequence of MCMY1 strain published in GenBank (PRJNA374601) as a target genome for comparison with other available B. thuringiensis genomes at the GenBank. Whole genome alignment, Fragment all-against-all comparison analysis, phylogenetic reconstruction and specific copper genes comparison were applied to all forty-five B. thuringiensis genomes to reveal the molecular adaptation to copper tolerance. The comparative results indicated that B. thuringiensis MCMY1 strain is closely related to strain Bt407 and strain IS5056. This strain harbors almost all available copper genes annotated from the forty-five B. thuringiensis genomes, except for the gene for Magnesium and cobalt efflux protein (CorC) which plays an indirect role in reducing the oxidative stress that caused by copper and other metal ions. Furthermore, the findings also showed that the Copper resistance gene family, CopABCDZ and its repressor (CsoR) are conserved in almost all sequenced genomes but the presence of the genes for Cytoplasmic copper homeostasis protein (CutC) and CorC across the sample genomes are highly inconsonant. The variation of these genes across the B. thuringiensis genomes suggests that each strain may have adapted to their specific ecological niche. However, further investigations will be need to support this preliminary hypothesis.

scholarly journals Differential Expression of the Three Multicopper Oxidases from Myxococcus xanthus

2007 ◽  
Vol 189 (13) ◽  
pp. 4887-4898 ◽  
Author(s):  
María Celestina Sánchez-Sutil ◽  
Nuria Gómez-Santos ◽  
Aurelio Moraleda-Muñoz ◽  
Lígia O. Martins ◽  
Juana Pérez ◽  
...  
Keyword(s):  
Adaptive Response ◽  
Growth And Development ◽  
Normal Development ◽  
Myxococcus Xanthus ◽  
Copper Resistance ◽  
Copper Tolerance ◽  
Deletion Mutants ◽  
Fruiting Bodies ◽  
Multicopper Oxidases ◽  
Copper Addition

ABSTRACT Myxococcus xanthus is a soil bacterium that undergoes a unique life cycle among the prokaryotes upon starvation, which includes the formation of macroscopic structures, the fruiting bodies, and the differentiation of vegetative rods into coccoid myxospores. This peculiarity offers the opportunity to study the copper response in this bacterium in two different stages. In fact, M. xanthus vegetative rods exhibit 15-fold-greater resistance against copper than developing cells. However, cells preadapted to this metal reach the same levels of resistance during both stages. Analysis of the M. xanthus genome reveals that many of the genes involved in copper resistance are redundant, three of which encode proteins of the multicopper oxidase family (MCO). Each MCO gene exhibits a different expression profile in response to external copper addition. Promoters of cuoA and cuoB respond to Cu(II) ions during growth and development; however, they show a 10-fold-increased copper sensitivity during development. The promoter of cuoC shows copper-independent induction upon starvation, but it is copper up-regulated during growth. Phenotypic analyses of deletion mutants reveal that CuoB is involved in the primary copper-adaptive response; CuoA and CuoC are necessary for the maintenance of copper tolerance; and CuoC is required for normal development. These roles seem to be carried out through cuprous oxidase activity.

Intrinsically fluorescent gold nanoclusters stabilized within a copper storage protein that follow the Irving–Williams trend in metal ion sensing

The Analyst ◽  
2019 ◽  
Vol 144 (13) ◽  
pp. 3949-3958 ◽  
Author(s):  
Dhanashree Selvan ◽  
Pallavi Prasad ◽  
Skyler Crane ◽  
Abubkr Abuhagr ◽  
Richard Covington ◽  
...  
Keyword(s):  
Storage Protein ◽  
Metal Ion ◽  
Gold Nanoclusters ◽  
Gold Clusters ◽  
Ion Sensing ◽  
Metal Detection ◽  
Metal Ion Sensing ◽  
Copper Storage ◽  
Tunable Emission

A copper storage protein is used to synthesize gold clusters with tunable emission that follow the Irving–Williams series for metal detection.

scholarly journals Multiple Megaplasmids Confer Extremely High Levels of Metal Tolerance in Alteromonas Strains

2019 ◽  
Vol 86 (3) ◽  
Author(s):  
Kathleen D. Cusick ◽  
Shawn W. Polson ◽  
Gabriel Duran ◽  
Russell T. Hill
Keyword(s):  
Gene Transfer ◽  
Pseudomonas Syringae ◽  
Molecular Mechanisms ◽  
Metal Tolerance ◽  
Bioinformatic Analysis ◽  
Metal Resistance ◽  
Copper Resistance ◽  
The Other ◽  
Copper Tolerance ◽  
Content Type

ABSTRACT Alteromonas is a widely distributed genus of marine Gammaproteobacteria, with representatives shown to be key players in diverse processes, including biogeochemical cycling and biofouling of marine substrata. While Alteromonas spp. are early colonizers of copper-based antifouling paints on marine vessels, their mechanism of tolerance is poorly understood. PacBio whole-genome sequencing of Alteromonas macleodii strains CUKW and KCC02, isolated from Cu/Ni alloy test coupons submerged in oligotrophic coastal waters, indicated the presence of multiple megaplasmids (ca. 200 kb) in both. A pulsed-field gel electrophoresis method was developed and used to confirm the presence of multiple megaplasmids in these two strains; it was then used to screen additional Alteromonas strains for which little to no sequencing data exist. Plasmids were not detected in any of the other strains. Bioinformatic analysis of the CUKW and KCC02 plasmids identified numerous genes associated with metal resistance. Copper resistance orthologs from both the Escherichia coli Cue and Cus and Pseudomonas syringae Cop systems were present, at times as multiple copies. Metal growth assays in the presence of copper, cobalt, manganese, and zinc performed with 10 Alteromonas strains demonstrated the ability of CUKW and KCC02 to grow at metal concentrations inhibitory to all the other strains tested. This study reports multiple megaplasmids in Alteromonas strains. Bioinformatic analysis of the CUKW and KCC02 plasmids indicate that they harbor elements of the Tra system conjugation apparatus, although their type of mobility remains to be experimentally verified. IMPORTANCE Copper is commonly used as an antifouling agent on ship hulls. Alteromonas spp. are early colonizers of copper-based antifouling paint, but their mechanism of tolerance is poorly understood. Sequencing of A. macleodii strains isolated from copper test materials for marine ships indicated the presence of multiple megaplasmids. Plasmids serve as key vectors in horizontal gene transfer and confer traits such as metal resistance, detoxification, ecological interaction, and antibiotic resistance. Bioinformatic analysis identified many metal resistance genes and genes associated with mobility. Understanding the molecular mechanisms and capacity for gene transfer within marine biofilms provides a platform for the development of novel antifouling solutions targeting genes involved in copper tolerance and biofilm formation.

scholarly journals Homology- and coevolution-consistent structural models of bacterial copper-tolerance protein CopM support a ‘metal sponge’ function and suggest regions for metal-dependent protein-protein interactions

2015 ◽  
Author(s):  
Luciano A. Abriata
Keyword(s):  
Protein Interactions ◽  
Binding Sites ◽  
Biochemical Characterization ◽  
Structural Models ◽  
Copper Resistance ◽  
Copper Tolerance ◽  
Copper Binding ◽  
Protein Protein Interactions ◽  
Disordered Regions ◽  
Copper Binding Sites

AbstractCopper is essential for life but toxic, therefore all organisms control tightly its intracellular abundance. Bacteria have indeed whole operons devoted to copper resistance, with genes that code for efflux pumps, oxidases, etc. Recently, the CopM protein of the CopMRS operon was described as a novel important element for copper tolerance in Synechocystis. This protein consists of a domain of unknown function, and was proposed to act as a periplasmic/extracellular copper binder. This work describes a bioinformatic study of CopM including structural models based on homology modeling and on residue coevolution, to help expand on its recent biochemical characterization. The protein is predicted to be periplasmic but membrane-anchored, not secreted. Two disordered regions are predicted, both possibly involved in protein-protein interactions. The 3D models disclose a 4-helix bundle with several potential copper-binding sites, most of them largely buried inside the bundle lumen. Some of the predicted copper-binding sites involve residues from the disordered regions, suggesting they could gain structure upon copper binding and thus possibly modulate the interactions they mediate. All models are provided as PDB files in the Supporting Information and can be visualized online at http://lucianoabriata.altervista.org/modelshome.htmlNote (January 2017): Recent X-ray structures of apo, copper- and silver-bound CopM are < 3Å RMSD away from the models, and reveal metal-dependent structural flexibility (Zhao et al Acta Crystallogr D Struct Biol. 2016)

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