Journal
FEBS LETTERS
Volume 584, Issue 6, Pages 1263-1267Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2010.02.041
Keywords
Viperin; Antiviral; Radical SAM; Iron-sulfur cluster; Metalloenzyme; S-Adenosylmethionine
Funding
- NIH [GM54608, RR-020185]
- Montana NSF EPSCOR [EPS-0701906]
- NASA Astrobiology Institute [NAI05-19]
Ask authors/readers for more resources
Viperin, an interferon-inducible antiviral protein, is shown to bind an iron-sulfur cluster, based on iron analysis as well as UV-Vis and electron paramagnetic resonance spectroscopic data. The reduced protein contains a [4Fe-4S](1+) cluster whose g-values are altered upon addition of S-adenosylmethionine (SAM), consistent with SAM coordination to the cluster. Incubation of reduced viperin with SAM results in reductive cleavage of SAM to produce 5'-deoxyadenosine (5'-dAdo), a reaction characteristic of the radical SAM superfamily. The 5'-dAdo cleavage product was identified by a combination of HPLC and mass spectrometry analysis. (C) 2010 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available