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Dbp5p/Rat8p is a yeast nuclear pore‐associated DEAD‐box protein essential for RNA export
Author(s) -
SnayHodge Christine A.,
Colot Hildur V.,
Goldstein Alan L.,
Cole Charles N.
Publication year - 1998
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/17.9.2663
Subject(s) - biology , dead box , yeast , nuclear pore , rna , nuclear protein , rna binding protein , nuclear export signal , saccharomyces cerevisiae , microbiology and biotechnology , genetics , computational biology , gene , transcription factor , nucleus , helicase
To identify Saccharomyces cerevisiae genes important for nucleocytoplasmic export of messenger RNA, we screened mutant strains to identify those in which poly(A) + RNA accumulated in nuclei under nonpermissive conditions. We describe the identification of DBP5 as the gene defective in the strain carrying the rat8‐1 allele ( RAT = ribonucleic acid trafficking). Dbp5p/Rat8p, a previously uncharacterized member of the DEAD‐box family of proteins, is closely related to eukaryotic initiation factor 4A(eIF4A) an RNA helicase essential for protein synthesis initiation. Analysis of protein databases suggests most eukaryotic genomes encode a DEAD‐box protein that is probably a homolog of yeast Dbp5p/Rat8p. Temperature‐sensitive alleles of DBP5/RAT8 were prepared. In rat8 mutant strains, cells displayed rapid, synchronous accumulation of poly(A) + RNA in nuclei when shifted to the non‐permissive temperature. Dbp5p/Rat8p is located within the cytoplasm and concentrated in the perinuclear region. Analysis of the distribution of Dbp5p/Rat8p in yeast strains where nuclear pore complexes are tightly clustered indicated that a fraction of this protein associates with nuclear pore complexes (NPCs). The strong mutant phenotype, association of the protein with NPCs and genetic interaction with factors involved in RNA export provide strong evidence that Dbp5p/Rat8p plays a direct role in RNA export.