@article{fdi:010085889,
  title = {{A} flexible and original architecture of two unrelated {Z}inc fingers underlies the role of the multitask {P}1 in {RYMV} spread},
  author = {{P}oignavent, {V}. and {H}oh, {F}. and {T}erral, {G}. and {Y}ang, {Y}. {S}. and {G}illet, {F}. {X}. and {K}im, {J}. {H}. and {A}llemand, {F}. and {L}acombe, {E}. and {B}rugidou, {C}hristophe and {C}ianferani, {S}. and {D}{\'e}m{\'e}n{\'e}, {H}. and {V}ignols, {F}.},
  editor = {},
  language = {{ENG}},
  abstract = {{V}iruses of the sobemovirus genus are plant viruses, most of which generate very important agricultural and financial losses. {A}mong them, the rice yellow mottle virus ({RYMV}) is one of the most damaging pathogens devastating rice fields in {A}frica. {RYMV} infectivity and propagation rely on its protein {P}1, identified as a key movement and potential long-distance {RNA} silencing suppressor. {H}ere we describe {P}1's complete 3{D} structure and dynamics obtained by an integrative approach combining {X}-{R}ay crystallography and {NMR} spectroscopy. {W}e show that {P}1 is organized in two semi-independent and topologically unrelated domains, each harboring an original zinc finger. {T}he two domains exhibit different affinities for zinc and sensitivities to oxidoreduction conditions, making the {C}-terminal {P}1 region a potential labile sensor of the plant redox status. {A}n additional level of regulation resides on the capacity of {P}1 to oligomerize through its {N}-terminal domain. {C}oupling {P}1 structure information with site-directed mutagenesis and plant functional assays, we identified key residues in each zinc domain essential for infectivity and spread in rice tissues. {A}ltogether, our results provide the first complete structure of a sobemoviral {P}1 movement protein and highlight structural and dynamical properties that may serve {RYMV} functions to infect and invade its host plant.},
  keywords = {3{D} structure ; {O}ryza sativa ; {S}obemovirus ; viral movement protein ; zinc finger protein},
  booktitle = {},
  journal = {{J}ournal of {M}olecular {B}iology},
  volume = {434},
  numero = {16},
  pages = {167715 [14 ]},
  ISSN = {0022-2836},
  year = {2022},
  DOI = {10.1016/j.jmb.2022.167715},
  URL = {https://www.documentation.ird.fr/hor/fdi:010085889},
}