| Literature DB >> 10617624 |
B Kosova1, N Panté, C Rollenhagen, A Podtelejnikov, M Mann, U Aebi, E Hurt.
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.Entities:
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Year: 2000 PMID: 10617624 DOI: 10.1074/jbc.275.1.343
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157