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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Biological Transport
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Cell Compartmentation
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Cell Nucleus / metabolism*
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Cell Nucleus / ultrastructure
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Fungal Proteins / genetics
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Fungal Proteins / isolation & purification
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Fungal Proteins / metabolism*
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Glutaral
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Membrane Proteins*
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Molecular Sequence Data
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Mutation
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Nuclear Envelope / chemistry
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Nuclear Envelope / metabolism*
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Nuclear Pore Complex Proteins
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Nuclear Proteins / isolation & purification
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Nuclear Proteins / metabolism*
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Protein Binding
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RNA, Messenger / metabolism
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RNA-Binding Proteins
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Recombinant Proteins / metabolism
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Saccharomyces cerevisiae Proteins*
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Spheroplasts
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Tissue Fixation
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Ultraviolet Rays / adverse effects
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Yeasts / metabolism
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Yeasts / radiation effects
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alpha Karyopherins
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beta Karyopherins
Substances
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Fungal Proteins
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MLP1 protein, S cerevisiae
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MLP2 protein, S cerevisiae
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Membrane Proteins
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NIC96 protein, S cerevisiae
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Nuclear Pore Complex Proteins
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Nuclear Proteins
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RNA, Messenger
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RNA-Binding Proteins
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Recombinant Proteins
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Saccharomyces cerevisiae Proteins
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alpha Karyopherins
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beta Karyopherins
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Glutaral