@article{fdi:010060558,
  title = {{T}he {RYMV}-encoded viral suppressor of {RNA} silencing {P}1 is a zinc-binding protein with redox-dependent flexibility},
  author = {{G}illet, {F}. {X}. and {C}attoni, {D}. {I}. and {P}etiot-{B}ecard, {S}. and {D}elalande, {F}. and {P}oignavent, {V}. and {B}rizard, {J}ean-{P}aul and {B}essin, {Y}. and {V}an {D}orsselaer, {A}. and {D}eclerck, {N}. and {S}anglier-{C}ianferani, {S}. and {B}rugidou, {C}hristophe and {V}ignols, {F}.},
  editor = {},
  language = {{ENG}},
  abstract = {{V}iral suppressors of {RNA} interference ({VSR}s) 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. {H}owever, the molecular mechanisms of {VSR}s are poorly understood. {W}e provide here biochemical and biophysical features of the dual suppressor/activator {VSR} {P}1 protein encoded by the rice yellow mottle virus. {I}n silico analyses of {P}1 suggested common features with zinc finger proteins and native mass spectrometry unambiguously confirmed that recombinant {P}1 binds reversibly two zinc atoms, each with a different strength. {A}dditionally, we demonstrate that the reaction of {P}1 with {H}2{O}2 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 {VSR}s. {T}hose reported here for {P}1 might be a general feature of {C}ys-rich {VSR}s and could be a key regulatory mechanism for the control of {RNA} silencing.},
  keywords = {gene silencing ; oxidative stress ; viral suppressor of {RNA}i ; zinc ; binding ; {RYMV}},
  booktitle = {},
  journal = {{J}ournal of {M}olecular {B}iology},
  volume = {425},
  numero = {14},
  pages = {2423--2435},
  ISSN = {0022-2836},
  year = {2013},
  DOI = {10.1016/j.jmb.2013.03.028},
  URL = {https://www.documentation.ird.fr/hor/fdi:010060558},
}