Cargando…
Mutations in domain IV of elongation factor EF-G confer −1 frameshifting
A recent crystal structure of a ribosome complex undergoing partial translocation in the absence of elongation factor EF-G showed disruption of codon–anticodon pairing and slippage of the reading frame by −1, directly implicating EF-G in preservation of the translational reading frame. Among mutatio...
Autores principales: | Niblett, Dustin, Nelson, Charlotte, Leung, Calvin S., Rexroad, Gillian, Cozy, Jake, Zhou, Jie, Lancaster, Laura, Noller, Harry F. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory Press
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7749637/ https://www.ncbi.nlm.nih.gov/pubmed/33008838 http://dx.doi.org/10.1261/rna.077339.120 |
Ejemplares similares
-
The role of GTP hydrolysis by EF-G in ribosomal translocation
por: Rexroad, Gillian, et al.
Publicado: (2022) -
Frameshifting at collided ribosomes is modulated by elongation factor eEF3 and by integrated stress response regulators Gcn1 and Gcn20
por: Houston, Lisa, et al.
Publicado: (2022) -
EF-G catalyzed translocation dynamics in the presence of ribosomal frameshifting stimulatory signals
por: Kim, Hee-Kyung, et al.
Publicado: (2017) -
Structural basis for +1 ribosomal frameshifting during EF-G-catalyzed translocation
por: Demo, Gabriel, et al.
Publicado: (2021) -
An eukaryotic elongation factor 2 from Medicago falcata (MfEF2) confers cold tolerance
por: Shi, Haifan, et al.
Publicado: (2019)