Subcellular localization and self-interaction of plant-specific Nt-4/1 protein.

摘要: The Nicotiana tabacum Nt-4/1 protein is a plant-specific of unknown function. Analysis bacterially expressed in vitro revealed that the secondary structure mostly alpha-helical and suggested it could consist three structural domains. Earlier studies At-4/1, Arabidopsis thaliana-encoded ortholog Nt-4/1, demonstrated GFP-fused At-4/1 was capable polar localization plant cells, association with plasmodesmata, cell-to-cell transport. Together ability to interact virus movement protein, these data supported hypothesis involvement viral transport through plasmodesmata. Studies Nt-4/1-GFP fusion reported this paper localized cytoplasmic bodies, which were co-aligned actin filaments actin-dependent intracellular movement. being non-membrane structures, found plasma membrane, tubular endoplasmic reticulum endosome-like structures. Bimolecular fluorescence complementation experiments inhibition nuclear export showed nuclear-cytoplasmic signal (NES) identified by site-directed mutagenesis. NES mutant nucleoplasm forming spherical bodies. Immunogold labeling electron microscopy Nt-4/1-containing bodies structures containing differences their fine structure. In mammalian formed similar those for cell nuclei. Using dynamic laser light scattering microscopy, form multimeric complexes vitro.