Mtr10p functions as a nuclear import receptor for the mRNA-binding protein Npl3p.

MTR10, previously shown to be involved in mRNA export, was found in a synthetic lethal relationship with nucleoporin NUP85. Green fluorescent protein (GFP)-tagged Mtr10p localizes preferentially inside the nucleus, but a nuclear pore and cytoplasmic distribution is also evident. Purified Mtr10p forms a complex with Npl3p, an RNA-binding protein that ...
shuttles in and out of the nucleus. In mtr10 mutants, nuclear uptake of Npl3p is strongly impaired at the restrictive temperature, while import of a classic nuclear localization signal (NLS)-containing protein is not. Accordingly, the NLS within Npl3p is extended and consists of the RGG box plus a short and non-repetitive C-terminal tail. Mtr10p interacts in vitro with Gsp1p-GTP, but with low affinity. Interestingly, Npl3p dissociates from Mtr10p only by incubation with Ran-GTP plus RNA. This suggests that Npl3p follows a distinct nuclear import pathway and that intranuclear release from its specific import receptor Mtr10p requires the cooperative action of both Ran-GTP and newly synthesized mRNA.
Mesh Terms:
Amino Acid Sequence, Biological Transport, Cell Nucleus, Fungal Proteins, GTP-Binding Proteins, Green Fluorescent Proteins, Guanosine Triphosphate, Humans, Luminescent Proteins, Molecular Sequence Data, Monomeric GTP-Binding Proteins, Mutagenesis, Nuclear Envelope, Nuclear Pore Complex Proteins, Nuclear Proteins, Nucleocytoplasmic Transport Proteins, Porins, RNA, Messenger, RNA-Binding Proteins, Ribonucleoproteins, Saccharomyces cerevisiae Proteins, Temperature, ran GTP-Binding Protein
EMBO J.
Date: Apr. 15, 1998
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