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. 2002 Apr 5;277(14):12151-7.
doi: 10.1074/jbc.M109103200. Epub 2002 Jan 16.

Characterization of an unusual importin alpha binding motif in the borna disease virus p10 protein that directs nuclear import

Thorsten Wolff  1 , Gunhild Unterstab, Gudrun Heins, Juergen A Richt, Michael Kann
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Free article

Characterization of an unusual importin alpha binding motif in the borna disease virus p10 protein that directs nuclear import

Thorsten Wolff et al. J Biol Chem. .
Free article

Abstract

Nuclear import of many cellular and viral proteins is mediated by short nuclear localization signals (NLS) that are recognized by intracellular receptor proteins belonging to the importin/karyopherin alpha and beta families. The primary structure of NLS is not well defined, but most contain at least three basic amino acids and harbor the relative consensus sequence K(K/R)X(K/R). We have studied the nuclear import of the Borna disease virus p10 protein that lacks a canonical oligobasic NLS. It is shown that the p10 protein exhibits all characteristics of an actively transported molecule in digitonin-permeabilized cells. Import activity was found to reside in the 20 N-terminal p10 amino acids that are devoid of an NLS consensus motif. Unexpectedly, p10-dependent import was blocked by a peptide inhibitor of importin alpha-dependent nuclear translocation, and the transport activity of the p10 N-terminal domain was shown to correlate with the ability to bind to importin alpha. These findings suggest that nuclear import of the Borna disease virus p10 protein occurs through a nonconventional karyophilic signal and highlight that the cellular importin alpha NLS receptor proteins can recognize nuclear targeting signals that substantially deviate from the consensus sequence.

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