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J Biol Chem, Vol. 275, Issue 1, 343-350, January 7, 2000
From BZH, Biochemie-Zentrum Heidelberg, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany
A fraction of the yeast nucleoporin Nic96p is
localized at the terminal ring of the nuclear basket. When Nic96p was
affinity purified from glutaraldehyde-treated spheroplasts, it was
found to be associated with Mlp2p. Mlp2p, together with Mlp1p, are the yeast Tpr homologues, which form the nuclear pore-attached intranuclear filaments (Strambio-de-Castillia, C., Blobel, G., and Rout, M. P. (1999) J. Cell Biol. 144, 839-855). Double disruption
mutants of MLP1 and MLP2 are viable and
apparently not impaired in nucleocytoplasmic transport. However,
overproduction of MLP1 causes nuclear accumulation of
poly(A)+ RNA in a chromatin-free area of the nucleus.
Mlp2p, A Component of Nuclear Pore Attached Intranuclear
Filaments, Associates with Nic96p*
,,
*
This work was supported in part by grants from the Human
Frontiers Science Program (HFSP) (to U. A. and E. C. H.), the M. E. Müller Foundation of Switzerland, and the
Swiss National Science Foundation (to N. P.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: Institute of Biochemistry, Swiss Federal
Institute of Technology (ETH), Universitätsstr. 16, CH-8092
Zürich, Switzerland.
§
Present address: CEBI Odense University, Staermosegaardsvej 16, DK-5230 Odense, Denmark.
¶
Present address: M. E. Müller Institute for
Microscopy, Biozentrum, University of Basel, CH-4056 Basel, Switzerland.
Recipient of Deutsche Forschungsgemeinschaft Grant SFB352. To
whom all correspondence should be addressed. Tel.: 49-6221-54-41-73; Fax: 49-6221-54-43-69; E-mail: cg5@ix.urz.uni-heidelberg.de.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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