Tags

Type your tag names separated by a space and hit enter

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.
EMBO J. 1999 Aug 02; 18(15):4332-47.EJ

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.

Links

PMC Free PDF
PMC Free Full Text

Authors+Show Affiliations

Schmitt C
University of Geneva, Department of Molecular Biology, 30 quai Ernest-Ansermet, CH-1205 Geneva.
von Kobbe C
No affiliation info available
Bachi A
No affiliation info available
Panté N
No affiliation info available
Rodrigues JP
No affiliation info available
Boscheron C
No affiliation info available
Rigaut G
No affiliation info available
Wilm M
No affiliation info available
Séraphin B
No affiliation info available
Carmo-Fonseca M
No affiliation info available
Izaurralde E
No affiliation info available

MeSH

Adenosine TriphosphatasesAmino Acid SequenceBiological TransportCloning, MolecularConserved SequenceCytoplasmDEAD-box RNA HelicasesEvolution, MolecularFungal ProteinsHeLa CellsHumansMembrane ProteinsMolecular Sequence DataMutagenesis, Site-DirectedNuclear EnvelopeNuclear Pore Complex ProteinsNuclear ProteinsNucleocytoplasmic Transport ProteinsRNA HelicasesRNA, MessengerRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsSequence Homology, Amino Acid

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

10428971

Citation

Schmitt, C, et al. "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." The EMBO Journal, vol. 18, no. 15, 1999, pp. 4332-47.
Schmitt C, von Kobbe C, Bachi A, et al. 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. EMBO J. 1999;18(15):4332-47.
Schmitt, C., von Kobbe, C., Bachi, A., Panté, N., Rodrigues, J. P., Boscheron, C., Rigaut, G., Wilm, M., Séraphin, B., Carmo-Fonseca, M., & Izaurralde, E. (1999). 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. The EMBO Journal, 18(15), 4332-47.
Schmitt C, et al. 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. EMBO J. 1999 Aug 2;18(15):4332-47. PubMed PMID: 10428971.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - 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. AU - Schmitt,C, AU - von Kobbe,C, AU - Bachi,A, AU - Panté,N, AU - Rodrigues,J P, AU - Boscheron,C, AU - Rigaut,G, AU - Wilm,M, AU - Séraphin,B, AU - Carmo-Fonseca,M, AU - Izaurralde,E, PY - 1999/8/3/pubmed PY - 1999/8/3/medline PY - 1999/8/3/entrez SP - 4332 EP - 47 JF - The EMBO journal JO - EMBO J VL - 18 IS - 15 N2 - 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. SN - 0261-4189 UR - https://www.unboundmedicine.com/medline/citation/10428971/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_ L2 - https://doi.org/10.1093/emboj/18.15.4332 DB - PRIME DP - Unbound Medicine ER -