Gillet F. X. auteur aut IRD Cattoni D. I. auteur aut IRD Petiot-Becard S. auteur aut IRD Delalande F. auteur aut IRD Poignavent V. auteur aut IRD Brizard Jean-Paul auteur aut IRD Bessin Y. auteur aut IRD Van Dorsselaer A. auteur aut IRD Declerck N. auteur aut IRD Sanglier-Cianferani S. auteur aut IRD Brugidou Christophe auteur aut IRD Vignols F. auteur aut IRD text journalArticle eng text/pdf born digital access Viral suppressors of RNA interference (VSRs) target host gene silencing pathways, thereby operating important roles in the viral cycle and in host cells, in which they counteract host innate immune responses. However, the molecular mechanisms of VSRs are poorly understood. We provide here biochemical and biophysical features of the dual suppressor/activator VSR P1 protein encoded by the rice yellow mottle virus. In silico analyses of P1 suggested common features with zinc finger proteins and native mass spectrometry unambiguously confirmed that recombinant P1 binds reversibly two zinc atoms, each with a different strength. Additionally, we demonstrate that the reaction of P1 with H2O2 leads to zinc release, disulfide bond formation, and protein oligomerization. A reversible protein modification by redox alterations has only been described for a limited number of zinc finger proteins and has never been reported for VSRs. Those reported here for P1 might be a general feature of Cys-rich VSRs and could be a key regulatory mechanism for the control of RNA silencing. specialized gene silencing oxidative stress viral suppressor of RNAi zinc binding RYMV 020 076 425 14 2423-2435 2013 0022-2836 https://www.documentation.ird.fr/hor/fdi:010060558 10.1016/j.jmb.2013.03.028 0022-2836 [F B010060558] https://www.documentation.ird.fr/hor/fdi:010060558 https://www.documentation.ird.fr/intranet/publi/2013/09/010060558.pdf Accès réservé (Intranet de l'IRD) IRD - Base Horizon / Pleins textes 2013-10-02 2017-08-23 fdi:010060558 fre