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Vol. 9, Issue 12, 3475-3492, December 1998
§ and
*Centre National de la Recherche Scientifique, UMR144,
Institut Curie, 75 248 Paris cedex 05, France; and
Nup159p/Rat7p is an essential FG repeat-containing nucleoporin
localized at the cytoplasmic face of the nuclear pore complex (NPC) and
involved in poly(A)+ RNA export and NPC distribution. A
detailed structural-functional analysis of this nucleoporin previously
demonstrated that Nup159p is anchored within the NPC through its
essential carboxyl-terminal domain. In this study, we demonstrate that
Nup159p specifically interacts through this domain with both Nsp1p and
Nup82p. Further analysis of the interactions within the
Nup159p/Nsp1p/Nup82p subcomplex using the nup82Department of Biochemistry, Dartmouth Medical School,
Hanover, New Hampshire 03755
108
mutant strain revealed that a deletion within the carboxyl-terminal
domain of Nup82p prevents its interaction with Nsp1p but does not
affect the interaction between Nup159p and Nsp1p. Moreover,
immunofluorescence analysis demonstrated that Nup159p is delocalized
from the NPC in nup82108 cells grown at 37°C, a
temperature at which the Nup82108p mutant protein becomes degraded.
This suggests that Nup82p may act as a docking site for a core complex
composed of the repeat-containing nucleoporins Nup159p and Nsp1p. In
vivo transport assays further revealed that nup82108
and nup159-1/rat7-1 mutant strains have little if any defect in nuclear protein import and protein export. Together our data
suggest that the poly(A)+ RNA export defect previously
observed in nup82 mutant cells might be due to the loss
from the NPCs of the repeat-containing nucleoporin Nup159p.
These authors contributed equally to this study.
Corresponding author. E-mail address:
vdoye{at}curie.fr.
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