Arginine/serine repeats are sufficient to constitute a splicing activation domain
AUTOR(ES)
Philipps, Dana
FONTE
Oxford University Press
RESUMO
SR proteins are essential pre-mRNA splicing factors that have been shown to bind a number of exonic splicing enhancers where they function to stimulate the splicing of adjacent introns. Members of the SR protein family contain one or two N-terminal RNA binding domains, as well as a C-terminal arginine–serine (RS) rich domain. The RS domains mediate protein–protein interactions with other RS domain containing proteins and are essential for many, but not all, SR protein functions. Hybrid proteins containing an RS domain fused to the bacteriophage MS2 coat protein are sufficient to activate enhancer-dependent splicing in HeLa cell nuclear extract when bound to the pre-mRNA. Here we report progress towards determining the protein sequence requirements for RS domain function. We show that the RS domains from non-SR proteins can also function as splicing activation domains when tethered to the pre-mRNA. Truncation experiments with the RS domain of the human SR protein 9G8 identified a 29 amino acid segment, containing 26 arginine or serine residues, that is sufficient to activate splicing when fused to MS2. We also show that synthetic domains composed solely of RS dipeptides are capable of activating splicing, although their potency is proportional to their size.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=275541Documentos Relacionados
- Identification of an snRNP-associated kinase activity that phosphorylates arginine/serine rich domains typical of splicing factors.
- Interaction between the N-terminal domain of human DNA topoisomerase I and the arginine-serine domain of its substrate determines phosphorylation of SF2/ASF splicing factor.
- An amino acid sequence motif sufficient for subnuclear localization of an arginine/serine-rich splicing factor.
- Characterization of a novel arginine/serine-rich splicing factor in Arabidopsis.
- Identification and Characterization of a Novel Serine-Arginine-Rich Splicing Regulatory Protein