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Friedrich Miescher Institute, PO Box 2543,CH-4002 Basel, Switzerland1
Institut für Biologie II, Zellbiologie, Universität Freiburg, 79104 Freiburg, Germany2
Institute of Genetics, Martin-Luther University, 06120 Halle, Germany3
Centre de Recherche en Infectiologie, Université Laval, Ste-Foy, Qc, G1V 4G2, Canada4
Author for correspondence: Thomas Hohn. Fax +41 61 6973976. e-mail hohn{at}fmi.ch
The mature cauliflower mosaic virus (CaMV) capsid protein (CP), if expressed in the absence of other viral proteins, is transported into the plant cell nucleus by the action of a nuclear localization signal (NLS) close to the N terminus. In contrast, virus particles do not enter the nucleus, but dock at the nuclear membrane, a process inhibited by anti-NLS antibodies or by GTP
S, and apparently mediated by interaction of CP with host importin
. The very acidic N-terminal extension of the viral CP precursor inhibits nuclear targeting of the protein and hence the precursor is localized in the cytoplasm. We hypothesize that this provides a control mechanism which ensures that the CP precursor is used for virus assembly in the cytoplasm and that only mature virus particles reach the nuclear pore.
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