The NPI-1/NPI-3 (Karyopherin alpha) binding site on the influenza A virus nucleoprotein NP is a nonconventional nuclear localization signal

被引：208

作者：

Wang, P ^{[1
]}

Palese, P ^{[1
]}

ONeill, RE ^{[1
]}

机构：

[1] CUNY MT SINAI SCH MED,DEPT MICROBIOL,NEW YORK,NY 10029

来源：

JOURNAL OF VIROLOGY | 1997年 / 71卷 / 03期

关键词：

D O I：

10.1128/JVI.71.3.1850-1856.1997

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Two cellular proteins, NPI-1 and NPI-3, were previously identified through their interaction with the influenza virus nucleoprotein (NP) by using the yeast two-hybrid system, These proteins were then shown to act as general transport factors (karyopherin alpha) and nuclear pore-docking proteins to facilitate the transport of the NP and of viral RNA into the nucleus. The yeast two-hybrid assay has now been used to identify the specific domains on the NP that bind to the NPI proteins. Mutational analysis including alanine scanning identified the motifs SxGTKRSYxxM and TKRSxxxM, which are required for binding to NPI-1 and NPI-3, respectively, These sequences were shown to possess nuclear localization signal (NLS) activity following expression of fusion proteins in HeLa cells, These sequences represent a novel nonconventional NLS motif. Another NLS activity not mediated by the NPI binding sites is associated with noncontiguous sequences in the NP.

引用

页码：1850 / 1856

页数：7

共 28 条

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