PMID- 10610322
OWN - NLM
STAT- MEDLINE
DCOM- 19991206
LR  - 20131121
IS  - 0261-4189 (Print)
IS  - 0261-4189 (Linking)
VI  - 18
IP  - 20
DP  - 1999 Oct 15
TI  - The RNA export factor Gle1p is located on the cytoplasmic fibrils of the NPC and 
      physically interacts with the FG-nucleoporin Rip1p, the DEAD-box protein
      Rat8p/Dbp5p and a new protein Ymr 255p.
PG  - 5761-77
AB  - Gle1p is an essential, nuclear pore complex (NPC)-associated RNA export factor.
      In a screen for high copy suppressors of a GLE1 mutant strain, we identified the 
      FG-nucleoporin Rip1p and the DEAD-box protein Rat8p/Dbp5p, both of which have
      roles in RNA export; we also found Ymr255p/Gfd1p, a novel inessential protein.
      All three high copy suppressors interact with the C-terminal domain of Gle1p;
      immunoelectron microscopy localizations indicate that Gle1p, Rip1p and
      Rat8p/Dbp5p are present on the NPC cytoplasmic fibrils; Rip1p was also found
      within the nucleoplasm and on the nuclear baskets. In vivo localizations support 
      the hypothesis that Rip1p contributes to the association of Gle1p with the pore
      and that Gle1p, in turn, provides a binding site for Rat8p/Dbp5p at the NPC.
      These data are consistent with the view that Gle1p, Rip1p, Rat8p/Dbp5p and
      Ymr255p/Gfd1p associate on the cytoplasmic side of the NPC to act in a terminal
      step of RNA export. We also describe a human functional homologue of Rip1p,
      called hCG1, which rescues Rip1p function in yeast, consistent with the
      evolutionary conservation of this NPC-associated protein.
FAU - Strahm, Y
AU  - Strahm Y
AD  - Microbiology Institute, CHUV, Lausanne.
FAU - Fahrenkrog, B
AU  - Fahrenkrog B
FAU - Zenklusen, D
AU  - Zenklusen D
FAU - Rychner, E
AU  - Rychner E
FAU - Kantor, J
AU  - Kantor J
FAU - Rosbach, M
AU  - Rosbach M
FAU - Stutz, F
AU  - Stutz F
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - EMBO J
JT  - The EMBO journal
JID - 8208664
RN  - 0 (Carrier Proteins)
RN  - 0 (DNA Primers)
RN  - 0 (Fungal Proteins)
RN  - 0 (GLE1 protein, S cerevisiae)
RN  - 0 (NUP42 protein, S cerevisiae)
RN  - 0 (Nuclear Pore Complex Proteins)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Nucleocytoplasmic Transport Proteins)
RN  - 0 (RNA-Binding Proteins)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - EC 3.6.1.- (Adenosine Triphosphatases)
RN  - EC 3.6.1.- (DBP5 protein, S cerevisiae)
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/*metabolism
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Carrier Proteins/*metabolism
MH  - Cytoplasm/metabolism
MH  - DEAD-box RNA Helicases
MH  - DNA Primers/genetics
MH  - Fungal Proteins/*metabolism
MH  - Humans
MH  - Mice
MH  - Microscopy, Immunoelectron
MH  - Molecular Sequence Data
MH  - Mutation
MH  - Nuclear Envelope/*metabolism
MH  - Nuclear Pore Complex Proteins
MH  - Nuclear Proteins/genetics/*metabolism
MH  - *Nucleocytoplasmic Transport Proteins
MH  - *RNA Helicases
MH  - RNA-Binding Proteins/*metabolism
MH  - Saccharomyces cerevisiae/genetics/metabolism
MH  - *Saccharomyces cerevisiae Proteins
MH  - Sequence Homology, Amino Acid
MH  - Suppression, Genetic
MH  - Temperature
PMC - PMC1171643
EDAT- 1999/12/28 00:00
MHDA- 1999/12/28 00:01
CRDT- 1999/12/28 00:00
PHST- 1999/12/28 00:00 [pubmed]
PHST- 1999/12/28 00:01 [medline]
PHST- 1999/12/28 00:00 [entrez]
AID - 10.1093/emboj/18.20.5761 [doi]
PST - ppublish
SO  - EMBO J. 1999 Oct 15;18(20):5761-77. doi: 10.1093/emboj/18.20.5761.