p54nrb/NonO and PSF promote U snRNA nuclear export by accelerating its export complex assembly
Author(s) -
Hiroto Izumi,
Asako McCloskey,
Kaori Shinmyozu,
Mutsuhito Ohno
Publication year - 2014
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/gkt1365
Subject(s) - snrnp , small nuclear rna , biology , nuclear export signal , biogenesis , microbiology and biotechnology , prp24 , ran , rna , ribonucleoprotein , cell nucleus , genetics , rna splicing , nucleus , non coding rna , gene
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 m(7)G-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.
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