p54nrb/NonO and PSF promote U snRNA nuclear export by accelerating its export complex assembly
| Autor: | Kaori Shinmyozu, Mutsuhito Ohno, Hiroto Izumi, Asako McCloskey |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Cytoplasm
Nucleocytoplasmic Transport Proteins Xenopus genetic processes Active Transport Cell Nucleus information science Receptors Cytoplasmic and Nuclear RNA-binding protein Karyopherins Biology environment and public health Nuclear Matrix-Associated Proteins RNA Small Nuclear Genetics Animals Humans snRNP PTB-Associated Splicing Factor Nuclear export signal SnRNP Biogenesis Cell Nucleus urogenital system RNA-Binding Proteins RNA Phosphoproteins Cell biology DNA-Binding Proteins ran GTP-Binding Protein Ran health occupations Octamer Transcription Factors Small nuclear RNA HeLa Cells |
| Zdroj: | Nucleic Acids Research |
| ISSN: | 0305-1048 |
| Popis: | The assembly of spliceosomal U snRNPs in metazoans requires nuclear export of U snRNA precursors. Four factors, nuclear cap-binding complex (CBC), phosphorylated adaptor for RNA export (PHAX), the export receptor CRM1 and RanGTP, gather at the m7G-cap-proximal region and form the U snRNA export complex. Here we show that the multifunctional RNA-binding proteins p54nrb/NonO and PSF are U snRNA export stimulatory factors. These proteins, likely as a heterodimer, accelerate the recruitment of PHAX, and subsequently CRM1 and Ran onto the RNA substrates in vitro, which mediates efficient U snRNA export in vivo. Our results reveal a new layer of regulation for U snRNA export and, hence, spliceosomal U snRNP biogenesis. |
| Databáze: | OpenAIRE |
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