The antiviral protein viperin is a radical SAM enzyme

被引:103
作者
Duschene, Kaitlin S.
Broderick, Joan B. [1 ]
机构
[1] Montana State Univ, Dept Chem & Biochem, Bozeman, MT 59717 USA
关键词
Viperin; Antiviral; Radical SAM; Iron-sulfur cluster; Metalloenzyme; S-Adenosylmethionine; LYASE-ACTIVATING ENZYME; IRON-SULFUR CLUSTER; GENE-EXPRESSION; BIOTIN SYNTHASE; INFLUENZA-VIRUS; LIPID RAFTS; ADENOSYLMETHIONINE; SUPERFAMILY; BINDING; IDENTIFICATION;
D O I
10.1016/j.febslet.2010.02.041
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:1263 / 1267
页数:5
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