Cargando…
DEAD-box RNA helicase domains exhibit a continuum between complete functional independence and high thermodynamic coupling in nucleotide and RNA duplex recognition
DEAD-box helicases catalyze the non-processive unwinding of double-stranded RNA (dsRNA) at the expense of adenosine triphosphate (ATP) hydrolysis. Nucleotide and RNA binding and unwinding are mediated by the RecA domains of the helicase core, but their cooperation in these processes remains poorly u...
Autores principales: | Samatanga, Brighton, Klostermeier, Dagmar |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4176333/ https://www.ncbi.nlm.nih.gov/pubmed/25123660 http://dx.doi.org/10.1093/nar/gku747 |
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) -
A conformational change in the helicase core is necessary but not sufficient for RNA unwinding by the DEAD box helicase YxiN
por: Karow, Anne R., et al.
Publicado: (2009) -
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) -
The GyrA-box determines the geometry of DNA bound to gyrase and couples DNA
binding to the nucleotide cycle
por: Lanz, Martin A., et al.
Publicado: (2012)