Technical note: Copper chaperone for copper, zinc superoxide dismutase: A potential biomarker for copper status in cattle1

2009 ◽  
Vol 87 (12) ◽  
pp. 4161-4166 ◽  
Author(s):  
J. J. Hepburn ◽  
J. D. Arthington ◽  
S. L. Hansen ◽  
J. W. Spears ◽  
M. D. Knutson
Keyword(s):  
Superoxide Dismutase ◽  
Technical Note ◽  
Copper Chaperone ◽  
Copper Zinc Superoxide Dismutase ◽  
Zinc Superoxide Dismutase ◽  
Copper Status ◽  
Potential Biomarker ◽  
Copper Zinc

scholarly journals The Copper Chaperone CCS Directly Interacts with Copper/Zinc Superoxide Dismutase

1998 ◽  
Vol 273 (37) ◽  
pp. 23625-23628 ◽  
Author(s):  
Ruby Leah B. Casareno ◽  
Darrel Waggoner ◽  
Jonathan D. Gitlin
Keyword(s):  
Superoxide Dismutase ◽  
Copper Chaperone ◽  
Copper Zinc Superoxide Dismutase ◽  
Zinc Superoxide Dismutase ◽  
Copper Zinc

scholarly journals The yeast copper chaperone for copper-zinc superoxide dismutase (CCS1) is a multifunctional chaperone promoting all levels of SOD1 maturation

2018 ◽  
Vol 294 (6) ◽  
pp. 1956-1966 ◽  
Author(s):  
Stefanie D. Boyd ◽  
Jenifer S. Calvo ◽  
Li Liu ◽  
Morgan S. Ullrich ◽  
Amélie Skopp ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Copper Chaperone ◽  
Copper Zinc Superoxide Dismutase ◽  
Zinc Superoxide Dismutase ◽  
Copper Zinc

scholarly journals The Megavirus Chilensis Cu,Zn-Superoxide Dismutase: the First Viral Structure of a Typical Cellular Copper Chaperone-Independent Hyperstable Dimeric Enzyme

2014 ◽  
Vol 89 (1) ◽  
pp. 824-832 ◽  
Author(s):  
Audrey Lartigue ◽  
Bénédicte Burlat ◽  
Bruno Coutard ◽  
Florence Chaspoul ◽  
Jean-Michel Claverie ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Crystallographic Structure ◽  
Copper Chaperone ◽  
Content Type ◽  
Copper Zinc Superoxide Dismutase ◽  
Zinc Superoxide Dismutase ◽  
Activity Measurements ◽  
Copper Zinc ◽  
Giant Viruses

ABSTRACTGiant viruses able to replicate inAcanthamoeba castellaniipenetrate their host through phagocytosis. After capsid opening, a fusion between the internal membranes of the virion and the phagocytic vacuole triggers the transfer in the cytoplasm of the viral DNA together with the DNA repair enzymes and the transcription machinery present in the particles. In addition, the proteome analysis of purified mimivirus virions revealed the presence of many enzymes meant to resist oxidative stress and conserved in theMimiviridae. Megavirus chilensis encodes a predicted copper, zinc superoxide dismutase (Cu,Zn-SOD), an enzyme known to detoxify reactive oxygen species released in the course of host defense reactions. While it was thought that the metal ions are required for the formation of the active-site lid and dimer stabilization, megavirus chilensis SOD forms a very stable metal-free dimer. We used electron paramagnetic resonance (EPR) analysis and activity measurements to show that the supplementation of the bacterial culture with copper and zinc during the recombinant expression of Mg277 is sufficient to restore a fully active holoenzyme. These results demonstrate that the viral enzyme's activation is independent of a chaperone both for disulfide bridge formation and for copper incorporation and suggest that its assembly may not be as regulated as that of its cellular counterparts. A SOD protein is encoded by a variety of DNA viruses but is absent from mimivirus. As in poxviruses, the enzyme might be dispensable when the virus infectsAcanthamoebacells but may allow megavirus chilensis to infect a broad range of eukaryotic hosts.IMPORTANCEMimiviridaeare giant viruses encoding more than 1,000 proteins. The virion particles are loaded with proteins used by the virus to resist the vacuole's oxidative stress. The megavirus chilensis virion contains a predicted copper, zinc superoxide dismutase (Cu,Zn-SOD). The corresponding gene is present in some megavirus chilensis relatives but is absent from mimivirus. This first crystallographic structure of a viral Cu,Zn-SOD highlights the features that it has in common with and its differences from cellular SODs. It corresponds to a very stable dimer of the apo form of the enzyme. We demonstrate that upon supplementation of the growth medium with Cu and Zn, the recombinant protein is fully active, suggesting that the virus's SOD activation is independent of a copper chaperone for SOD generally used by eukaryotic SODs.

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