PMID- 10428971
OWN - NLM
STAT- MEDLINE
DCOM- 19990916
LR  - 20131121
IS  - 0261-4189 (Print)
IS  - 0261-4189 (Linking)
VI  - 18
IP  - 15
DP  - 1999 Aug 2
TI  - 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.
PG  - 4332-47
AB  - 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.
FAU - Schmitt, C
AU  - Schmitt C
AD  - University of Geneva, Department of Molecular Biology, 30 quai Ernest-Ansermet,
      CH-1205 Geneva.
FAU - von Kobbe, C
AU  - von Kobbe C
FAU - Bachi, A
AU  - Bachi A
FAU - Pante, N
AU  - Pante N
FAU - Rodrigues, J P
AU  - Rodrigues JP
FAU - Boscheron, C
AU  - Boscheron C
FAU - Rigaut, G
AU  - Rigaut G
FAU - Wilm, M
AU  - Wilm M
FAU - Seraphin, B
AU  - Seraphin B
FAU - Carmo-Fonseca, M
AU  - Carmo-Fonseca M
FAU - Izaurralde, E
AU  - Izaurralde E
LA  - eng
SI  - GENBANK/AJ237946
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - EMBO J
JT  - The EMBO journal
JID - 8208664
RN  - 0 (Fungal Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (NUP159 protein, S cerevisiae)
RN  - 0 (Nuclear Pore Complex Proteins)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Nucleocytoplasmic Transport Proteins)
RN  - 0 (RNA, Messenger)
RN  - 0 (RNA-Binding Proteins)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - EC 3.6.1.- (Adenosine Triphosphatases)
RN  - EC 3.6.1.- (DDX19B protein, human)
RN  - EC 3.6.4.13 (DEAD-box RNA Helicases)
RN  - EC 3.6.4.13 (RNA Helicases)
SB  - IM
MH  - Adenosine Triphosphatases/genetics/*metabolism
MH  - Amino Acid Sequence
MH  - Biological Transport
MH  - Cloning, Molecular
MH  - Conserved Sequence
MH  - Cytoplasm/*metabolism
MH  - DEAD-box RNA Helicases
MH  - Evolution, Molecular
MH  - Fungal Proteins/genetics/metabolism
MH  - HeLa Cells
MH  - Humans
MH  - Membrane Proteins/*metabolism
MH  - Molecular Sequence Data
MH  - Mutagenesis, Site-Directed
MH  - Nuclear Envelope/*metabolism
MH  - *Nuclear Pore Complex Proteins
MH  - Nuclear Proteins/*metabolism
MH  - *Nucleocytoplasmic Transport Proteins
MH  - *RNA Helicases
MH  - RNA, Messenger/genetics/*metabolism
MH  - RNA-Binding Proteins/genetics/*metabolism
MH  - *Saccharomyces cerevisiae Proteins
MH  - Sequence Homology, Amino Acid
PMC - PMC1171509
EDAT- 1999/08/03 00:00
MHDA- 1999/08/03 00:01
CRDT- 1999/08/03 00:00
PHST- 1999/08/03 00:00 [pubmed]
PHST- 1999/08/03 00:01 [medline]
PHST- 1999/08/03 00:00 [entrez]
AID - 10.1093/emboj/18.15.4332 [doi]
PST - ppublish
SO  - EMBO J. 1999 Aug 2;18(15):4332-47. doi: 10.1093/emboj/18.15.4332.