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- Title
The antiviral protein viperin is a radical SAM enzyme
- Authors
Duschene, Kaitlin S.; Broderick, Joan B.
- Abstract
Abstract: 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.
- Subjects
ANTIVIRAL agents; IRON-sulfur proteins; IRON analysis; ELECTRON paramagnetic resonance spectroscopy; CLUSTER analysis (Statistics); HIGH performance liquid chromatography; MASS spectrometry; ADENOSYLMETHIONINE; THERAPEUTICS
- Publication
FEBS Letters, 2010, Vol 584, Issue 6, p1263
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2010.02.041