@article{fdi:010042530,
  title = {{C}haracterization of a ribonuclease {III}-like protein required for cleavage of the pre-r{RNA} in the 3 ' {ETS} in {A}rabidopsis},
  author = {{C}omella, {P}. and {P}ontvianne, {F}. and {L}ahmy, {S}. and {V}ignols, {F}. and {B}arbezier, {N}. and {D}e{B}ures, {A}. and {J}obet, {E}. and {B}rugidou, {C}hristophe and {E}cheverria, {M}. and {S}aez {V}asquez, {J}.},
  editor = {},
  language = {{ENG}},
  abstract = {{R}ibonuclease {III} ({RN}ase{III}) is responsible for processing and maturation of {RNA} precursors into functional r{RNA}, m{RNA} and other small {RNA}. {I}n contrast to bacterial and yeast cells, higher eukaryotes contain at least three classes of {RN}ase{III}, including class {IV} or dicer-like proteins. {H}ere, we describe the functional characterization of {A}t{RTL}2, an {A}rabidopsis thaliana {RN}ase{III}-like protein that belongs to a small family of genes distinct from the dicer family. {W}e demonstrate that {A}t{RTL}2 is required for 3external transcribed spacer ({ETS}) cleavage of the pre-r{RNA} in vivo. {A}t{RTL}2 localizes in the nucleus and cytoplasm, a nuclear export signal ({NES}) in the {N}-terminal sequence probably controlling {A}t{RTL}2 cellular localization. {T}he modeled 3{D} structure of the {RN}ase{III} domain of {A}t{RTL}2 is similar to the bacterial {RN}ase{III} domain, suggesting a comparable catalytic mechanism. {H}owever, unlike bacterial {RN}ase{III}, the {A}t{RTL}2 protein forms a highly salt-resistant homodimer that is only disrupted on treatment with {DTT}. {T}hese data indicate that {A}t{RTL}2 may use a dimeric mechanism to cleave double-stranded {RNA}, but unlike bacterial or yeast {RN}ase {III} proteins, {A}t{RTL}2 forms homodimers through formation of disulfide bonds, suggesting that redox conditions may operate to regulate the activity of {RN}ase{III}.},
  keywords = {},
  booktitle = {},
  journal = {{N}ucleic {A}cids {R}esearch},
  volume = {36},
  numero = {4},
  pages = {1163--1175},
  ISSN = {0305-1048},
  year = {2008},
  DOI = {10.1093/nar/gkm1130},
  URL = {https://www.documentation.ird.fr/hor/fdi:010042530},
}