Dbp5, a DEAD-box protein required for mRNA export, is recruited to the cytoplasmic fibrils of nuclear pore complex via a conserved interaction with CAN/Nup159p - PubMed (original) (raw)

Dbp5, a DEAD-box protein required for mRNA export, is recruited to the cytoplasmic fibrils of nuclear pore complex via a conserved interaction with CAN/Nup159p

C Schmitt et al. EMBO J. 1999.

Abstract

Dbp5 is a DEAD-box protein essential for mRNA export from the nucleus in yeast. Here we report the isolation of a cDNA encoding human Dbp5 (hDbp5) which is 46% identical to yDbp5p. Like its yeast homologue, hDbp5 is localized within the cytoplasm and at the nuclear rim. By immunoelectron microscopy, the nuclear envelope-bound fraction of Dbp5 has been localized to the cytoplasmic fibrils of the nuclear pore complex (NPC). Consistent with this localization, we show that both the human and yeast proteins directly interact with an N-terminal region of the nucleoporins CAN/Nup159p. In a conditional yeast strain in which Nup159p is degraded when shifted to the nonpermissive temperature, yDbp5p dissociates from the NPC and localizes to the cytoplasm. Thus, Dbp5 is recruited to the NPC via a conserved interaction with CAN/Nup159p. To investigate its function, we generated defective hDbp5 mutants and analysed their effects in RNA export by microinjection in Xenopus oocytes. A mutant protein containing a Glu-->Gln change in the conserved DEAD-box inhibited the nuclear exit of mRNAs. Together, our data indicate that Dbp5 is a conserved RNA-dependent ATPase which is recruited to the cytoplasmic fibrils of the NPC where it participates in the export of mRNAs out of the nucleus.

PubMed Disclaimer

Cited by

RNA Export through the NPC in Eukaryotes.
Okamura M, Inose H, Masuda S. Okamura M, et al. Genes (Basel). 2015 Mar 20;6(1):124-49. doi: 10.3390/genes6010124. Genes (Basel). 2015. PMID: 25802992 Free PMC article. Review.
Systems-level analyses identify extensive coupling among gene expression machines.
Maciag K, Altschuler SJ, Slack MD, Krogan NJ, Emili A, Greenblatt JF, Maniatis T, Wu LF. Maciag K, et al. Mol Syst Biol. 2006;2:2006.0003. doi: 10.1038/msb4100045. Epub 2006 Jan 17. Mol Syst Biol. 2006. PMID: 16738550 Free PMC article.
Small bristles, the Drosophila ortholog of NXF-1, is essential for mRNA export throughout development.
Wilkie GS, Zimyanin V, Kirby R, Korey C, Francis-Lang H, Van Vactor D, Davis I. Wilkie GS, et al. RNA. 2001 Dec;7(12):1781-92. RNA. 2001. PMID: 11780634 Free PMC article.
Degradation of endogenous proteins and generation of a null-like phenotype in zebrafish using Trim-Away technology.
Chen X, Liu M, Lou H, Lu Y, Zhou MT, Ou R, Xu Y, Tang KF. Chen X, et al. Genome Biol. 2019 Jan 23;20(1):19. doi: 10.1186/s13059-019-1624-4. Genome Biol. 2019. PMID: 30674345 Free PMC article.
From unwinding to clamping - the DEAD box RNA helicase family.
Linder P, Jankowsky E. Linder P, et al. Nat Rev Mol Cell Biol. 2011 Jul 22;12(8):505-16. doi: 10.1038/nrm3154. Nat Rev Mol Cell Biol. 2011. PMID: 21779027 Review.

Dbp5, a DEAD-box protein required for mRNA export, is recruited to the cytoplasmic fibrils of nuclear pore complex via a conserved interaction with CAN/Nup159p - PubMed (original) (raw)