ArticleProtein science : a publication of the Protein Society2016
The acidic domain is a unique structural feature of the splicing factor SYNCRIP.
Article in Protein science : a publication of the Protein Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Survival-Related Genes on Chromosomes 6 and 17 in Medulloblastoma.International journal of molecular sciences · 2024Article
- Adenosine Triphosphate: The Primordial Molecule That Controls Protein Homeostasis and Shapes the Genome-Proteome Interface.Biomolecules · 2024Review
- Emerging Roles of RNA-Binding Proteins in Neurodevelopment.Journal of developmental biology · 2022Review
- SYNCRIP facilitates porcine parvovirus viral DNA replication through the alternative splicing of NS1 mRNA to promote NS2 mRNA formation.Veterinary research · 2021Article
- RNA-binding protein syncrip regulates starvation-induced hyperactivity in adult Drosophila.PLoS genetics · 2021Article
- Exploring the RNA landscape of endothelial exosomes.RNA (New York, N.Y.) · 2018Article
- A cryptic RNA-binding domain mediates Syncrip recognition and exosomal partitioning of miRNA targets.Nature communications · 2018Article
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Authors and funding
4 authors.
Funding
Abstract
The splicing factor SYNCRIP (hnRNP Q) is involved in viral replication, neural morphogenesis, modulation of circadian oscillation, and the regulation of the cytidine deaminase APOBEC1. It consists of three globular RNA-recognition motifs (RRM) domains flanked by an N-terminal acid-rich acidic sequence segment domain (AcD12-97 ) and a C-terminal domain containing an arginine-glycine-rich sequence motif (RGG/RXG box), which are located near to the N- and C-terminals, respectively. The acid-rich sequence segment is unique to SYNCRIP and the closely related protein hnRNP R, and is involved in interactions with APOBEC1. Here, we show that while AcD12-97 does not form a globular domain, structure-based annotation identified a self-folding globular domain with an all α-helix architecture, AcD24-107 . The NMR structure of AcD24-107 is fundamentally different from previously reported AcD molecular models. In addition to negatively charged surface areas, it contains a large hydrophobic cavity and a positively charged surface area as potential epitopes for intermolecular interactions.
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