The acidic domain is a unique structural feature of the splicing factor SYNCRIP

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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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