Publications des scientifiques de l'IRD

Gillet F. X., Cattoni D. I., Petiot-Becard S., Delalande F., Poignavent V., Brizard Jean-Paul, Bessin Y., Van Dorsselaer A., Declerck N., Sanglier-Cianferani S., Brugidou Christophe, Vignols F. (2013). The RYMV-encoded viral suppressor of RNA silencing P1 is a zinc-binding protein with redox-dependent flexibility. Journal of Molecular Biology, 425 (14), p. 2423-2435. ISSN 0022-2836.

Titre du document
The RYMV-encoded viral suppressor of RNA silencing P1 is a zinc-binding protein with redox-dependent flexibility
Année de publication
2013
Type de document
Article référencé dans le Web of Science WOS:000321722800005
Auteurs
Gillet F. X., Cattoni D. I., Petiot-Becard S., Delalande F., Poignavent V., Brizard Jean-Paul, Bessin Y., Van Dorsselaer A., Declerck N., Sanglier-Cianferani S., Brugidou Christophe, Vignols F.
Source
Journal of Molecular Biology, 2013, 425 (14), p. 2423-2435 ISSN 0022-2836
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.
Plan de classement
Sciences fondamentales / Techniques d'analyse et de recherche [020] ; Sciences du monde végétal [076]
Localisation
Fonds IRD [F B010060558]
Identifiant IRD
fdi:010060558
Contact