Mlp2p, a component of nuclear pore attached intranuclear filaments, associates with Nic96p
Makaleler > Tam Makale · 2000
Yazarlar: Buket KOSOVA, NELLY PANTE, CHRISTIANE ROLLENHAGEN, ALEXANDRE PODTELEJNİKOV, M Mann, UELI AEBI, ED HURT
JOURNAL OF BIOLOGICAL CHEMISTRY, SCI Expanded İndekslerine Giren Dergi, Uluslararası, 2000, cilt 275, ss 343-350
Özet
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. (1499) 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.