@article{fdi:010052850,
  title = {{T}he {N}-terminal domain of the {A}renavirus {L} protein is an {RNA} endonuclease essential in m{RNA} transcription},
  author = {{M}orin, {B}. and {C}outard, {B}. and {L}elke, {M}. and {F}erron, {F}. and {K}erber, {R}. and {J}amal, {S}. and {F}rangeul, {A}. and {B}aronti, {C}{\'e}cile and {C}harrel, {R}. and de {L}amballerie, {X}avier and {V}onrhein, {C}. and {L}escar, {J}. and {B}ricogne, {G}. and {G}unther, {S}. and {C}anard, {B}.},
  editor = {},
  language = {{ENG}},
  abstract = {{A}renaviridae synthesize viral m{RNA}s using short capped primers presumably acquired from cellular transcripts by a 'cap-snatching' mechanism. {H}ere, we report the crystal structure and functional characterization of the {N}-terminal 196 residues ({NL}1) of the {L} protein from the prototypic arenavirus: lymphocytic choriomeningitis virus. {T}he {NL}1 domain is able to bind and cleave {RNA}. {T}he 2.13 angstrom resolution crystal structure of {NL}1 reveals a type {II} endonuclease alpha/beta architecture similar to the {N}-terminal end of the influenza virus {PA} protein. {S}uperimposition of both structures, mutagenesis and reverse genetics studies reveal a unique spatial arrangement of key active site residues related to the {PD}...({D}/{E}) {XK} type {II} endonuclease signature sequence. {W}e show that this endonuclease domain is conserved and active across the virus families {A}renaviridae, {B}unyaviridae and {O}rthomyxoviridae and propose that the arenavirus {NL}1 domain is the {A}renaviridae cap-snatching endonuclease.},
  keywords = {},
  booktitle = {},
  journal = {{P}los {P}athogens},
  volume = {6},
  numero = {9},
  pages = {e1001038},
  ISSN = {1553-7366},
  year = {2010},
  DOI = {10.1371/journal.ppat.1001038},
  URL = {https://www.documentation.ird.fr/hor/fdi:010052850},
}