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

被引：71

作者：

Kosova, B ^{[1
]}

Panté, N ^{[1
]}

Rollenhagen, C ^{[1
]}

Podtelejnikov, A ^{[1
]}

Mann, M ^{[1
]}

Aebi, U ^{[1
]}

Hurt, E ^{[1
]}

机构：

[1] Biochem Zentrum Heidelberg, D-69120 Heidelberg, Germany

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2000年 / 275卷 / 01期

关键词：

D O I：

10.1074/jbc.275.1.343

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：343 / 350

页数：8

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