Reference: Kosova B, et al. (2000) Mlp2p, a component of nuclear pore attached intranuclear filaments, associates with nic96p. J Biol Chem 275(1):343-50

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Abstract


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.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Kosova B, Panté N, Rollenhagen C, Podtelejnikov A, Mann M, Aebi U, Hurt E
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