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Mlp2p, a component of nuclear pore attached intranuclear filaments, associates with nic96p.
- Source :
- Journal of Biological Chemistry; January 2000, Vol. 275 Issue: 1 p343-50, 8p
- Publication Year :
- 2000
-
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.
Details
- Language :
- English
- ISSN :
- 00219258 and 1083351X
- Volume :
- 275
- Issue :
- 1
- Database :
- Supplemental Index
- Journal :
- Journal of Biological Chemistry
- Publication Type :
- Periodical
- Accession number :
- ejs7151699