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BIBTEX RIS

The antiviral protein viperin is a radical SAM enzyme

2010; Wiley; Volume: 584; Issue: 6 Linguagem: Inglês

10.1016/j.febslet.2010.02.041

ISSN

1873-3468

Autores

Kaitlin S. Duschene, Joan Broderick,

Tópico(s)

RNA modifications and cancer

Resumo

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.

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