Nup192p is a conserved nucleoporin with a preferential location at the inner site of the nuclear membrane
Human Nup93, the homologue of yeast Nic96p, is associated with a 205-kDa protein whose intracellular location and function is unknown. We show here that the yeast open reading frame YJL039c, which is homologous to this human p205, encodes the so far largest yeast nucleoporin. Accordingly, green fluo...
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Veröffentlicht in: | The Journal of biological chemistry 1999-08, Vol.274 (32), p.22646-22651 |
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Sprache: | eng |
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Zusammenfassung: | Human Nup93, the homologue of yeast Nic96p, is associated with a 205-kDa protein whose intracellular location and function
is unknown. We show here that the yeast open reading frame YJL039c, which is homologous to this human p205, encodes the so
far largest yeast nucleoporin. Accordingly, green fluorescent protein (GFP)-tagged YJL039c was localized to the nuclear pores
and therefore named Nup192p. Affinity purification of ProtA-Nic96p from glutaraldehyde-fixed spheroplasts reveals association
with Nup192p. NUP192 is essential for cell growth. A temperature-sensitive mutant nup192â15 is neither impaired in nuclear import of a SV40 nuclear
localization sequence-containing reporter protein nor in mRNA export, but association of Nup49-GFP with nuclear pores is inhibited
at the non-permissive temperature. By immunoelectron microscopy, Nup192p-ProtA is seen at the inner site of the nuclear pores,
at a distance of 60 ± 15 nm from the central plane of the pore. This suggests that Nup192p is an evolutionarily conserved
structural component of the nuclear pore complex with a preferential location at the inner site of the nuclear membrane. |
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ISSN: | 0021-9258 1083-351X |
DOI: | 10.1074/jbc.274.32.22646 |