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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-...

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Detalles Bibliográficos
Autores principales:	Galaz-Davison, Pablo, Román, Ernesto A., Ramírez-Sarmiento, César A.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Public Library of Science 2021
Materias:	Research Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8454952/ https://www.ncbi.nlm.nih.gov/pubmed/34478435 http://dx.doi.org/10.1371/journal.pcbi.1008882

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