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.

• Publication year

  2000

• Venue

  Journal of Biological Chemistry

• Publication date

  2000-01-07

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1074/jbc.275.1.343PMID 10617624
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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