Musashi-1: An example of how polyalanine tracts contribute to self-association in the intrinsically disordered regions of RNA-binding proteins

Tsai Chen Chen, Jie Rong Huang*

*此作品的通信作者

研究成果: Article同行評審

12 引文 斯高帕斯(Scopus)

摘要

RNA-binding proteins (RBPs) have intrinsically disordered regions (IDRs) whose biophysical properties have yet to be explored to the same extent as those of the folded RNA interacting domains. These IDRs are essential to the formation of biomolecular condensates, such as stress and RNA granules, but dysregulated assembly can be pathological. Because of their structural heterogeneity, IDRs are best studied by NMR spectroscopy. In this study, we used NMR spectroscopy to investigate the structural propensity and self-association of the IDR of the RBP Musashi-1. We identified two transient α-helical regions (residues ~208–218 and ~270–284 in the IDR, the latter with a polyalanine tract). Strong NMR line broadening in these regions and circular dichroism and micrography data suggest that the two α-helical elements and the hydrophobic residues in between may contribute to the formation of oligomers found in stress granules and implicated in Alzheimer’s disease. Bioinformatics analysis suggests that polyalanine stretches in the IDRs of RBPs may have evolved to promote RBP assembly.

原文English
文章編號2289
期刊International Journal Of Molecular Sciences
21
發行號7
DOIs
出版狀態Published - 1 4月 2020

指紋

深入研究「Musashi-1: An example of how polyalanine tracts contribute to self-association in the intrinsically disordered regions of RNA-binding proteins」主題。共同形成了獨特的指紋。

引用此