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      Nuclear export of mRNA by TAP/NXF1 requires two nucleoporin-binding sites but not p15.

      Molecular and Cellular Biology
      ATP-Binding Cassette Transporters, Active Transport, Cell Nucleus, physiology, Animals, Binding Sites, Carrier Proteins, metabolism, Cell Line, Cell Nucleus, Drosophila Proteins, Drosophila melanogaster, Humans, Mutagenesis, Site-Directed, Nuclear Pore Complex Proteins, Nuclear Proteins, genetics, Nucleocytoplasmic Transport Proteins, Oocytes, cytology, Protein Binding, Protein Structure, Tertiary, RNA, Messenger, RNA-Binding Proteins, Recombinant Fusion Proteins, Sequence Deletion, Structure-Activity Relationship, Xenopus laevis

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          Abstract

          Metazoan NXF1/p15 heterodimers promote export of bulk mRNA through nuclear pore complexes (NPC). NXF1 interacts with the NPC via two distinct structural domains, the UBA-like domain and the NTF2-like scaffold, which results from the heterodimerization of the NTF2-like domain of NXF1 with p15. Both domains feature a single nucleoporin-binding site, and they act synergistically to promote NPC translocation. Whether the NTF2-like scaffold (and thereby p15) contributes only to NXF1/NPC association or is also required for other functions, e.g., to impart directionality to the export process by regulating NXF1/NPC or NXF1/cargo interactions, remains unresolved. Here we show that a minimum of two nucleoporin-binding sites is required for NXF1-mediated export of cellular mRNA. These binding sites can be provided by an NTF2-like scaffold followed by a UBA-like domain (as in the wild-type protein) or by two NTF2-like scaffolds or two UBA-like domains in tandem. In the latter case, the export activity of NXF1 is independent of p15. Thus, as for the UBA-like domain, the function of the NTF2-like scaffold is confined to nucleoporin binding. More importantly, two copies of either of these domains are sufficient to promote directional transport of mRNA cargoes across the NPC.

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