The NPI-1/NPI-3 (karyopherin alpha) binding site on the influenza a virus nucleoprotein NP is a nonconventional nuclear localization signal-Reference-Cited by-同舟云学术

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

Published:1997-03 Issue:3 Volume:71 Page:1850-1856
ISSN:0022-538X
Container-title:Journal of Virology
language:en
Short-container-title:J Virol

Author:

Wang P¹,Palese P¹,O'Neill R E¹

Affiliation:

1. Department of Microbiology, Mount Sinai School of Medicine, New York, New York 10029, USA.

Abstract

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.

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/jvi.71.3.1850-1856.1997

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