Cargando…
Reversible fold-switching controls the functional cycle of the antitermination factor RfaH
RfaH, member of the NusG/Spt5 family, activates virulence genes in Gram-negative pathogens. RfaH exists in two states, with its C-terminal domain (CTD) folded either as α-helical hairpin or β-barrel. In free RfaH, the α-helical CTD interacts with, and masks the RNA polymerase binding site on, the N-...
Autores principales: | Zuber, Philipp Konrad, Schweimer, Kristian, Rösch, Paul, Artsimovitch, Irina, Knauer, Stefan H. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6370827/ https://www.ncbi.nlm.nih.gov/pubmed/30742024 http://dx.doi.org/10.1038/s41467-019-08567-6 |
Ejemplares similares
-
Functional regions of the N-terminal domain of the antiterminator RfaH
por: Belogurov, Georgiy A, et al.
Publicado: (2010) -
Interdomain contacts control folding of transcription factor RfaH
por: Tomar, Sushil Kumar, et al.
Publicado: (2013) -
Structural and thermodynamic analyses of the β-to-α transformation in RfaH reveal principles of fold-switching proteins
por: Zuber, Philipp K, et al.
Publicado: (2022) -
The universally-conserved transcription factor RfaH is recruited to a hairpin structure of the non-template DNA strand
por: Zuber, Philipp K, et al.
Publicado: (2018) -
Putative transcription antiterminator RfaH contributes to Erwinia amylovora virulence
por: Klee, Sara M., et al.
Publicado: (2022)