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.
Copyright 2010. Published by Elsevier B.V.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Antiviral Agents / isolation & purification
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Antiviral Agents / metabolism
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Cloning, Molecular
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Humans
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Hydrolases* / genetics
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Hydrolases* / isolation & purification
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Hydrolases* / metabolism
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Hydrolases* / physiology
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Hydrolysis
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In Vitro Techniques
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Iron / metabolism
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Models, Biological
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Oxidation-Reduction
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Oxidoreductases Acting on CH-CH Group Donors
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Protein Binding
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Proteins / genetics
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Proteins / isolation & purification
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Proteins / metabolism
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Proteins / physiology*
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S-Adenosylmethionine / chemistry
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S-Adenosylmethionine / metabolism
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Sulfur / metabolism
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Time Factors
Substances
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Antiviral Agents
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Proteins
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Sulfur
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S-Adenosylmethionine
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Iron
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Oxidoreductases Acting on CH-CH Group Donors
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RSAD2 protein, human
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Hydrolases
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adenosylmethionine hydrolase