Cargando…
Rbg1–Tma46 dimer structure reveals new functional domains and their role in polysome recruitment
Developmentally Regulated GTP-binding (DRG) proteins are highly conserved GTPases that associate with DRG Family Regulatory Proteins (DFRP). The resulting complexes have recently been shown to participate in eukaryotic translation. The structure of the Rbg1 GTPase, a yeast DRG protein, in complex wi...
Autores principales: | Francis, Sandrea M., Gas, María-Eugenia, Daugeron, Marie-Claire, Bravo, Jeronimo, Séraphin, Bertrand |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2012
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3510508/ https://www.ncbi.nlm.nih.gov/pubmed/23002146 http://dx.doi.org/10.1093/nar/gks867 |
Ejemplares similares
-
Structural consequences of the interaction of RbgA with a 50S ribosomal subunit assembly intermediate
por: Seffouh, Amal, et al.
Publicado: (2019) -
Gbp2 interacts with THO/TREX through a novel type of RRM domain
por: Martínez-Lumbreras, Santiago, et al.
Publicado: (2016) -
The highly conserved eukaryotic DRG factors are required for efficient translation in a manner redundant with the putative RNA helicase Slh1
por: Daugeron, Marie-Claire, et al.
Publicado: (2011) -
Structural analysis and dimerization profile of the SCAN domain of the pluripotency factor Zfp206
por: Liang, Yu, et al.
Publicado: (2012) -
Structural basis of dimerization and dual W-box DNA recognition by rice WRKY domain
por: Cheng, Xiankun, et al.
Publicado: (2019)