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Vol. 8, Issue 10, 2017-2038, October 1997
and
*Biochemie-Zentrum Heidelberg (BZH), University of Heidelberg,
D-69120 Heidelberg, Germany;
Yeast and vertebrate nuclear pores display significant
morphological similarity by electron microscopy, but sequence
similarity between the respective proteins has been more difficult to
observe. Herein we have identified a vertebrate nucleoporin, Nup93, in both human and Xenopus that has proved to be an
evolutionarily related homologue of the yeast nucleoporin Nic96p.
Polyclonal antiserum to human Nup93 detects corresponding proteins in
human, rat, and Xenopus cells. Immunofluorescence and
immunoelectron microscopy localize vertebrate Nup93 at the nuclear
basket and at or near the nuclear entry to the gated channel of the
pore. Immunoprecipitation from both mammalian and
Xenopus cell extracts indicates that a small fraction of
Nup93 physically interacts with the nucleoporin p62, just as yeast
Nic96p interacts with the yeast p62 homologue. However, a large
fraction of vertebrate Nup93 is extracted from pores and is also
present in Xenopus egg extracts in complex with a newly
discovered 205-kDa protein. Mass spectrometric sequencing of the human
205-kDa protein reveals that this protein is encoded by an open reading
frame, KIAAO225, present in the human database. The putative human
nucleoporin of 205 kDa has related sequence homologues in
Caenorhabditis elegans and Saccharomyces
cerevisiae. To analyze the role of the Nup93 complex in the
pore, nuclei were assembled that lack the Nup93 complex after
immunodepletion of a Xenopus nuclear reconstitution extract. The Nup93-complex-depleted nuclei are clearly defective for
correct nuclear pore assembly. From these experiments, we conclude that
the vertebrate and yeast pore have significant homology in their
functionally important cores and that, with the identification of Nup93
and the 205-kDa protein, we have extended the knowledge of the
nearest-neighbor interactions of this core in both yeast and
vertebrates.
Department of Molecular
Biology, University of Geneva Sciences II, 1211 Geneva, Switzerland;
Department of Biology, University of California at San
Diego, La Jolla, California;
§Maurice E. Müller
Institute, Biozentrum University of Basel, Switzerland; and
Protein & Peptide Group, European Molecular Biology
Laboratory, D-69115 Heidelberg, Germany
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