Cargando…
A conformational change in the helicase core is necessary but not sufficient for RNA unwinding by the DEAD box helicase YxiN
Cooperative binding of ATP and RNA to DEAD-box helicases induces the closed conformation of their helicase core, with extensive interactions across the domain interface. The bound RNA is bent, and its distortion may constitute the first step towards RNA unwinding. To dissect the role of the conforma...
Autores principales: | Karow, Anne R., Klostermeier, Dagmar |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2009
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2715247/ https://www.ncbi.nlm.nih.gov/pubmed/19474341 http://dx.doi.org/10.1093/nar/gkp397 |
Ejemplares similares
-
Allosteric regulation of helicase core activities of the DEAD-box helicase YxiN by RNA binding to its RNA recognition motif
por: Samatanga, Brighton, et al.
Publicado: (2017) -
The putative RNase P motif in the DEAD box helicase Hera is dispensable for efficient interaction with RNA and helicase activity
por: Linden, Martin H., et al.
Publicado: (2008) -
A novel dimerization motif in the C-terminal domain of the Thermus thermophilus DEAD box helicase Hera confers substantial flexibility(†)
por: Klostermeier, Dagmar, et al.
Publicado: (2009) -
DEAD-box RNA helicase domains exhibit a continuum between complete functional independence and high thermodynamic coupling in nucleotide and RNA duplex recognition
por: Samatanga, Brighton, et al.
Publicado: (2014) -
Insights into the mechanism of a G-quadruplex-unwinding DEAH-box helicase
por: Chen, Michael C., et al.
Publicado: (2015)