Author:
Farazi Thalia A.,Leonhardt Carl S.,Mukherjee Neelanjan,Mihailovic Aleksandra,Li Song,Max Klaas E.A.,Meyer Cindy,Yamaji Masashi,Cekan Pavol,Jacobs Nicholas C.,Gerstberger Stefanie,Bognanni Claudia,Larsson Erik,Ohler Uwe,Tuschl Thomas
Abstract
Recent studies implicated the RNA-binding protein with multiple splicing (RBPMS) family of proteins in oocyte, retinal ganglion cell, heart, and gastrointestinal smooth muscle development. These RNA-binding proteins contain a single RNA recognition motif (RRM), and their targets and molecular function have not yet been identified. We defined transcriptome-wide RNA targets using photoactivatable-ribonucleoside-enhanced crosslinking and immunoprecipitation (PAR-CLIP) in HEK293 cells, revealing exonic mature and intronic pre-mRNA binding sites, in agreement with the nuclear and cytoplasmic localization of the proteins. Computational and biochemical approaches defined the RNA recognition element (RRE) as a tandem CAC trinucleotide motif separated by a variable spacer region. Similar to other mRNA-binding proteins, RBPMS family of proteins relocalized to cytoplasmic stress granules under oxidative stress conditions suggestive of a support function for mRNA localization in large and/or multinucleated cells where it is preferentially expressed.
Publisher
Cold Spring Harbor Laboratory
Cited by
47 articles.
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