Intrinsically disordered RGG/RG domains mediate degenerate specificity in RNA binding.
Nucleic Acids Res
; 45(13): 7984-7996, 2017 Jul 27.
Article
em En
| MEDLINE
| ID: mdl-28575444
ABSTRACT
RGG/RG domains are the second most common RNA binding domain in the human genome, yet their RNA-binding properties remain poorly understood. Here, we report a detailed analysis of the RNA binding characteristics of intrinsically disordered RGG/RG domains from Fused in Sarcoma (FUS), FMRP and hnRNPU. For FUS, previous studies defined RNA binding as mediated by its well-folded domains; however, we show that RGG/RG domains are the primary mediators of binding. RGG/RG domains coupled to adjacent folded domains can achieve affinities approaching that of full-length FUS. Analysis of RGG/RG domains from FUS, FMRP and hnRNPU against a spectrum of contrasting RNAs reveals that each display degenerate binding specificity, while still displaying different degrees of preference for RNA.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
RNA
/
Proteínas Intrinsicamente Desordenadas
Tipo de estudo:
Prognostic_studies
Limite:
Animals
/
Humans
Idioma:
En
Ano de publicação:
2017
Tipo de documento:
Article