Artículo de revista
The DEAD-box helicase DDX3 substitutes for the cap-binding protein eIF4E to promote compartmentalized translation initiation of the HIV-1 genomic RNA
Fecha
2013Registro en:
Nucleic Acids Research, 2013, Vol. 41, No. 12
doi:10.1093/nar/gkt306
Autor
Soto Rifo, Ricardo
Rubilar, Paulina S.
Ohlmann, Théophile
Institución
Resumen
Here, we show a novel molecular mechanism
promoted by the DEAD-box RNA helicase DDX3 for
translation of the HIV-1 genomic RNA. This occurs
through the adenosine triphosphate-dependent formation
of a translation initiation complex that is
assembled at the 50 m7GTP cap of the HIV-1
mRNA. This is due to the property of DDX3 to
substitute for the initiation factor eIF4E in the
binding of the HIV-1 m7GTP 50 cap structure where
it nucleates the formation of a core DDX3/PABP/
eIF4G trimeric complex on the HIV-1 genomic RNA.
By using RNA fluorescence in situ hybridization
coupled to indirect immunofluorescence, we
further show that this viral ribonucleoprotein
complex is addressed to compartmentalized cytoplasmic
foci where the translation initiation
complex is assembled.