The N-terminal domain of RfaH plays an active role in protein fold-switching.
The bacterial elongation factor RfaH promotes the expression of virulence factors by specifically binding to RNA polymerases (RNAP) paused at a DNA signal. This behavior is unlike that of its paralog NusG, the major representative of the protein family to which RfaH belongs. Both proteins have an N-...
Guardado en:
Autores principales: | Pablo Galaz-Davison, Ernesto A Román, César A Ramírez-Sarmiento |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Public Library of Science (PLoS)
2021
|
Materias: | |
Acceso en línea: | https://doaj.org/article/1462933c4c2b499cbea461320e2947f8 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Reversible fold-switching controls the functional cycle of the antitermination factor RfaH
por: Philipp Konrad Zuber, et al.
Publicado: (2019) -
Origins and Molecular Evolution of the NusG Paralog RfaH
por: Bing Wang, et al.
Publicado: (2020) -
A Screen for <italic toggle="yes">rfaH</italic> Suppressors Reveals a Key Role for a Connector Region of Termination Factor Rho
por: Kuang Hu, et al.
Publicado: (2017) -
Structure of the C-terminal domain of TRADD reveals a novel fold in the death domain superfamily
por: Ning Zhang, et al.
Publicado: (2017) -
NMR structure of the Bacillus cereus hemolysin II C-terminal domain reveals a novel fold
por: Anne R. Kaplan, et al.
Publicado: (2017)