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The RYMV-encoded viral suppressor of RNA silencing P1 is a zinc-binding protein with redox-dependent flexibility.

Abstract：

: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.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Gillet FX,Cattoni DI,Petiot-Bécard S,Delalande F,Poignavent V,Brizard JP,Bessin Y,Dorsselaer AV,Declerck N,Sanglier-Cianférani S,Brugidou C,Vignols F

doi

10.1016/j.jmb.2013.03.028

subject

Has Abstract

pub_date

2013-07-24 00:00:00

pages

2423-35

issue

14

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(13)00191-5

journal_volume

425

pub_type

杂志文章

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