Mlp2p, a component of nuclear pore attached intranuclear filaments, associates with Nic96p

Creative Commons License

Kosova B. , PANTE N., ROLLENHAGEN C., PODTELEJNİKOV A., Mann M., AEBI U., ...Daha Fazla

JOURNAL OF BIOLOGICAL CHEMISTRY, cilt.275, ss.343-350, 2000 (SCI İndekslerine Giren Dergi) identifier identifier identifier

  • Cilt numarası: 275 Konu: 1
  • Basım Tarihi: 2000
  • Doi Numarası: 10.1074/jbc.275.1.343
  • Sayfa Sayıları: ss.343-350


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.