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J Biol Chem, Vol. 274, Issue 8, 5252-5258, February 19, 1999
From the Department of Cell Biology, University of Alberta,
Edmonton, Alberta T6G 2A7, Canada
Integral membrane proteins associated with the
nuclear pore complex (NPC) are likely to play an important role in the
biogenesis of this structure. Here we have examined the functional
roles of domains of the yeast pore membrane protein Pom152p in
establishing its topology and its interactions with other NPC proteins.
The topology of Pom152p was evaluated by alkaline extraction, protease protection, and endoglycosidase H sensitivity assays. The results of
these experiments suggest that Pom152p contains a single transmembrane segment with its N terminus (amino acid residues 1-175) extending into
the nuclear pore and its C terminus (amino acid residues 196-1337)
positioned in the lumen of the nuclear envelope. The functional role of
these different domains was investigated in mutants that are dependent
on Pom152p for viability. The requirement for Pom152p in strains
containing mutations allelic to the NPC protein genes NIC96
and NUP59 could be alleviated by Pom152p's N terminus,
independent of its integration into the membrane. However,
complementation of a mutation in NUP170 required both the N
terminus and the transmembrane segment. Furthermore, mutations in
NUP188 were rescued only by full-length Pom152p, suggesting that the lumenal structures play an important role in the function of
pore-side NPC structures.
Topology and Functional Domains of the Yeast Pore Membrane
Protein Pom152p
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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