Next Article in Journal
Knockout of the OsNAC006 Transcription Factor Causes Drought and Heat Sensitivity in Rice
Previous Article in Journal
Upregulation of CASP9 through NF-κB and Its Target MiR-1276 Contributed to TNFα-Promoted Apoptosis of Cancer Cells Induced by Doxorubicin
Previous Article in Special Issue
Spotlight on the Ballet of Proteins: The Structural Dynamic Properties of Proteins Illuminated by Solution NMR
Open AccessArticle

Musashi-1: An Example of How Polyalanine Tracts Contribute to Self-Association in the Intrinsically Disordered Regions of RNA-Binding Proteins

1
Institute of Biochemistry and Molecular Biology, National Yang-Ming University, No. 155 Section 2 Li-nong Street, Taipei 11221, Taiwan
2
Institute of Biomedical Informatics, National Yang-Ming University, No. 155 Section 2 Li-nong Street, Taipei 11221, Taiwan
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2020, 21(7), 2289; https://doi.org/10.3390/ijms21072289
Received: 3 March 2020 / Revised: 20 March 2020 / Accepted: 24 March 2020 / Published: 26 March 2020
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. View Full-Text
Keywords: RNA-binding proteins; intrinsically disordered proteins; polyalanine; liquid–liquid phase separation; self-association RNA-binding proteins; intrinsically disordered proteins; polyalanine; liquid–liquid phase separation; self-association
Show Figures

Figure 1

MDPI and ACS Style

Chen, T.-C.; Huang, J.-R. Musashi-1: An Example of How Polyalanine Tracts Contribute to Self-Association in the Intrinsically Disordered Regions of RNA-Binding Proteins. Int. J. Mol. Sci. 2020, 21, 2289.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop