Mlp2p, a component of nuclear pore attached intranuclear filaments, associates with nic96p.
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.
Mesh Terms:
Amino Acid Sequence, Biological Transport, Cell Compartmentation, Cell Nucleus, Fungal Proteins, Glutaral, Membrane Proteins, Molecular Sequence Data, Mutation, Nuclear Envelope, Nuclear Pore Complex Proteins, Nuclear Proteins, Protein Binding, RNA, Messenger, Recombinant Proteins, Saccharomyces cerevisiae Proteins, Spheroplasts, Tissue Fixation, Ultraviolet Rays, Yeasts, alpha Karyopherins, beta Karyopherins
Amino Acid Sequence, Biological Transport, Cell Compartmentation, Cell Nucleus, Fungal Proteins, Glutaral, Membrane Proteins, Molecular Sequence Data, Mutation, Nuclear Envelope, Nuclear Pore Complex Proteins, Nuclear Proteins, Protein Binding, RNA, Messenger, Recombinant Proteins, Saccharomyces cerevisiae Proteins, Spheroplasts, Tissue Fixation, Ultraviolet Rays, Yeasts, alpha Karyopherins, beta Karyopherins
J. Biol. Chem.
Date: Jan. 07, 2000
PubMed ID: 10617624
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