The RNA-binding complex ESCRT-II in Xenopus laevis eggs recognizes purine-rich sequences through its subunit, Vps25
| Autor: | Amy B. Emerman, Michael D. Blower |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Messenger RNA RNA localization biology Chemistry Xenopus RNA RNA-binding protein macromolecular substances Cell Biology biology.organism_classification Biochemistry ESCRT Cell biology VPS25 03 medical and health sciences 030104 developmental biology Gene expression Molecular Biology |
| Zdroj: | Journal of Biological Chemistry. 293:12593-12605 |
| ISSN: | 0021-9258 |
| Popis: | RNA-binding proteins (RBP) are critical regulators of gene expression. Recent studies have uncovered hundreds of mRNA-binding proteins that do not contain annotated RNA-binding domains and have well-established roles in other cellular processes. Investigation of these nonconventional RBPs is critical for revealing novel RNA-binding domains and may disclose connections between RNA regulation and other aspects of cell biology. The endosomal sorting complex required for transport II (ESCRT-II) is a nonconventional RNA-binding complex that has a canonical role in multivesicular body formation. ESCRT-II was identified previously as an RNA-binding complex in Drosophila oocytes, but whether its RNA-binding properties extend beyond Drosophila is unknown. In this study, we found that the RNA-binding properties of ESCRT-II are conserved in Xenopus eggs, where ESCRT-II interacted with hundreds of mRNAs. Using a UV cross-linking approach, we demonstrated that ESCRT-II binds directly to RNA through its subunit, Vps25. UV cross-linking and immunoprecipitation (CLIP)-Seq revealed that Vps25 specifically recognizes a polypurine (i.e. GA-rich) motif in RNA. Using purified components, we could reconstitute the selective Vps25-mediated binding of the polypurine motif in vitro. Our results provide insight into the mechanism by which ESCRT-II selectively binds to mRNA and also suggest an unexpected link between endosome biology and RNA regulation. |
| Databáze: | OpenAIRE |
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