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Vol. 9, Issue 2, 355-373, February 1998
Department of Cell Biology and Physiology, Washington University
School of Medicine, St. Louis, Missouri 63110
Integral membrane proteins are predicted to play key roles in the
biogenesis and function of nuclear pore complexes (NPCs). Revealing how
the transport apparatus is assembled will be critical for understanding
the mechanism of nucleocytoplasmic transport. We observed that
expression of the carboxyl-terminal 200 amino acids of the nucleoporin
Nup116p had no effect on wild-type yeast cells, but it rendered the
nup116 null strain inviable at all temperatures and
coincidentally resulted in the formation of nuclear membrane
herniations at 23°C. To identify factors related to NPC function, a
genetic screen for high-copy suppressors of this lethal nup116-C phenotype was conducted. One gene (designated
SNL1 for suppressor of
nup116-C lethal) was identified
whose expression was necessary and sufficient for rescuing growth.
Snl1p has a predicted molecular mass of 18.3 kDa, a putative
transmembrane domain, and limited sequence similarity to Pom152p, the
only previously identified yeast NPC-associated integral membrane
protein. By both indirect immunofluorescence microscopy and subcellular
fractionation studies, Snl1p was localized to both the nuclear envelope
and the endoplasmic reticulum. Membrane extraction and topology assays suggested that Snl1p was an integral membrane protein, with its carboxyl-terminal region exposed to the cytosol. With regard to genetic
specificity, the nup116-C lethality was also suppressed by high-copy GLE2 and NIC96. Moreover,
high-copy SNL1 suppressed the temperature sensitivity of
gle2-1 and nic96-G3 mutant cells. The
nic96-G3 allele was identified in a synthetic lethal
genetic screen with a null allele of the closely related nucleoporin
nup100. Gle2p physically associated with Nup116p in
vitro, and the interaction required the N-terminal region of Nup116p.
Therefore, genetic links between the role of Snl1p and at least three
NPC-associated proteins were established. We suggest that Snl1p plays a
stabilizing role in NPC structure and function.
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