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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Autores principales: Pablo Galaz-Davison, Ernesto A Román, César A Ramírez-Sarmiento
Formato: article
Lenguaje:EN
Publicado: Public Library of Science (PLoS) 2021
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Acceso en línea:https://doaj.org/article/1462933c4c2b499cbea461320e2947f8
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