In-cell NMR reveals potential precursor of toxic species from SOD1 fALS mutants.
Nat Commun. 2014;5:5502
Authors: Luchinat E, Barbieri L, Rubino JT, Kozyreva T, Cantini F, Banci L
Abstract
Mutations in the superoxide dismutase 1 (SOD1) gene are related to familial cases of amyotrophic lateral sclerosis (fALS). Here we exploit in-cell NMR to characterize the protein folding and maturation of a series of fALS-linked SOD1 mutants in human cells and to obtain insight into their behaviour in the cellular context, at the molecular level. The effect of various mutations on SOD1 maturation are investigated by changing the availability of metal ions in the cells, and by coexpressing the copper chaperone for SOD1, hCCS. We observe for most of the mutants the occurrence of an unstructured SOD1 species, unable to bind zinc. This species may be a common precursor of potentially toxic oligomeric species, that are associated with fALS. Coexpression of hCCS in the presence of copper restores the correct maturation of the SOD1 mutants and prevents the formation of the unstructured species, confirming that hCCS also acts as a molecular chaperone.
PMID: 25429517 [PubMed - as supplied by publisher]
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Pruning the ALS-Associated Protein SOD1 for in-CellNMR
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Jens Danielsson, Kohsuke Inomata, Shuhei Murayama, Hidehito Tochio, Lisa Lang, Masahiro Shirakawa and Mikael Oliveberg
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja404425r/aop/images/medium/ja-2013-04425r_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja404425r
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/XDAlpDiBNe4
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Read the rest at Spectroscopynow.com
In-cell NMR reveals potential precursor of toxic species from SOD1 fALS mutants.
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