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1: J Biol Chem. 2000 Jan 7;275(1):343-50.Click here to read Links

Mlp2p, a component of nuclear pore attached intranuclear filaments, associates with nic96p.

Kosova B, Panté N, Rollenhagen C, Podtelejnikov A, Mann M, Aebi U, Hurt E.

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.

PMID: 10617624 [PubMed - indexed for MEDLINE]