Organic phase separation opens up new opportunities to interrogate the RNA-binding proteome

Protein-RNA interactions regulate all aspects of RNA metabolism and are crucial to the function of catalytic ribonucleoproteins. Until recently, the available technologies to capture RNA-bound proteins have been biased toward poly(A) RNA-binding proteins (RBPs) or involve molecular labeling, limitin...

Full description

Saved in:
Bibliographic Details
Main Authors: Smith, Tom (Author) , Villanueva, Eneko (Author) , Queiroz, Rayner M. L. (Author) , Dawson, Charlotte S. (Author) , Elzek, Mohamed (Author) , Urdaneta Zurbarán, Erika Cristina (Author) , Willis, Anne E. (Author) , Beckmann, Benedikt M. (Author) , Krijgsveld, Jeroen (Author) , Lilley, Kathryn S. (Author)
Format: Article (Journal)
Language:English
Published: 1 March 2020
In: Current opinion in chemical biology
Year: 2020, Volume: 54, Pages: 70-75
ISSN:1879-0402
DOI:10.1016/j.cbpa.2020.01.009
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.cbpa.2020.01.009
Verlag, lizenzpflichtig, Volltext: http://www.sciencedirect.com/science/article/pii/S1367593120300107
Get full text
Author Notes:Tom Smith, Eneko Villanueva, Rayner M.L. Queiroz, Charlotte S. Dawson, Mohamed Elzek, Erika C. Urdaneta, Anne E. Willis, Benedikt M. Beckmann, Jeroen Krijgsveld, and Kathryn S. Lilley
Description
Summary:Protein-RNA interactions regulate all aspects of RNA metabolism and are crucial to the function of catalytic ribonucleoproteins. Until recently, the available technologies to capture RNA-bound proteins have been biased toward poly(A) RNA-binding proteins (RBPs) or involve molecular labeling, limiting their application. With the advent of organic-aqueous phase separation-based methods, we now have technologies that efficiently enrich the complete suite of RBPs and enable quantification of RBP dynamics. These flexible approaches to study RBPs and their bound RNA open up new research avenues for systems-level interrogation of protein-RNA interactions.
Item Description:Gesehen am 11.01.2021
Physical Description:Online Resource
ISSN:1879-0402
DOI:10.1016/j.cbpa.2020.01.009