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Figure 2


Fig. 2. The nucleolar localization of nucleostemin is gated by a nucleoplasmic-retaining mechanism independent of its nucleolus-targeting domains. (A1-E2) When fused to the N-terminus (A1) or the C-terminus (B1) of B23, the I-domain of nucleostemin significantly increased the amount of B23 in the nucleoplasm compared with the epitope-tagged (A2, B2) or the GFP-tagged proteins (A3, B3) at their respective ends. This nucleoplasmic-retaining activity of the I-domain could also be transferred to three ribosomal proteins, L5, L11 and L23. Unlike the nucleolar distributions of their original proteins (C2, D2, E2), the I-domain fusions of these proteins (C1, D1, E1) localized almost exclusively in the nucleoplasm. Anti-fibrillarin or anti-B23 immunostainings of the same cells are shown in the bottom panels. Fusion constructs are depicted at the bottom of each panel. Bars, 10 µm.





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