Cargando…
The DbpA catalytic core unwinds double-helix substrates by directly loading on them
DbpA is a DEAD-box RNA helicase implicated in the assembly of the large ribosomal subunit. Similar to all the members of the DEAD-box family, the DbpA protein has two N-terminal RecA-like domains, which perform the RNA unwinding. However, unlike other members of this family, the DbpA protein also po...
Autores principales: | Childs, Jared J., Gentry, Riley C., Moore, Anthony F.T., Koculi, Eda |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory Press
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4748818/ https://www.ncbi.nlm.nih.gov/pubmed/26755693 http://dx.doi.org/10.1261/rna.052928.115 |
Ejemplares similares
-
Time course of large ribosomal subunit assembly in E. coli cells overexpressing a helicase inactive DbpA protein
por: Gentry, Riley C., et al.
Publicado: (2016) -
Kinetics and Thermodynamics of DbpA Protein’s
C-Terminal Domain Interaction with RNA
por: López de Victoria, Aliana, et al.
Publicado: (2017) -
Structural basis for RNA-duplex unwinding by the DEAD-box helicase DbpA
por: Wurm, Jan Philip
Publicado: (2023) -
Structural basis for the activation of the DEAD-box RNA helicase DbpA by the nascent ribosome
por: Wurm, Jan Philip, et al.
Publicado: (2021) -
Resonance assignment and secondary structure of DbpA protein from the European species, Borrelia afzelii
por: Hejduk, Libor, et al.
Publicado: (2021)